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Concise Results
Standard Results
Full Results
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+)) [Escherichia coli str. K-12 substr. MG1655]
Protein Classification
NADP-dependent malic enzyme ( domain architecture ID 11482649 )
NADP-dependent malic enzyme catalyzes the conversion of (S)-malate to pyruvate and carbon dioxide using NADP as a cofactor
List of domain hits
Name
Accession
Description
Interval
E-value
PRK07232
PRK07232 bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
3-756
0e+00
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
Pssm-ID: 235976 [Multi-domain]
Cd Length: 752
Bit Score: 1534.27
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 3 D QLKQ S ALD F H E FP V PGKI Q V S PTKPLATQRDL A LAYSPGVAAPCLEI E KDP LK AYKYTARGNLVAVISNGTAVLGLGNI 82
Cdd:PRK07232 1 E QLKQ A ALD Y H R FP R PGKI E V T PTKPLATQRDL S LAYSPGVAAPCLEI A KDP AD AYKYTARGNLVAVISNGTAVLGLGNI 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 83 GALA G KPVMEGKGVLFKKFAGIDVFDIEVDE L DPDKFIE V VAALEPTFGGINLEDIKAPECFYIE Q KLRERM N IPVFHDD 162
Cdd:PRK07232 81 GALA S KPVMEGKGVLFKKFAGIDVFDIEVDE E DPDKFIE A VAALEPTFGGINLEDIKAPECFYIE E KLRERM D IPVFHDD 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 QHGTAIIS T AA I LN G L RV V E K N I S DV RM VVSGAGAAAIAC M NLLVALG LQ K H NI V VCDSKGVIY Q GR EPN M A E T KAAYAV 242
Cdd:PRK07232 161 QHGTAIIS A AA L LN A L EL V G K K I E DV KI VVSGAGAAAIAC L NLLVALG AK K E NI I VCDSKGVIY K GR TEG M D E W KAAYAV 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 243 v D DGK RTL DDV IEGAD I FLG C S GPK VLT Q EMVK K MA RA P M I L ALANP E PEI L P PL AK E VRPDAII C TGRSDYPNQVNNVL 322
Cdd:PRK07232 241 - D TDA RTL AEA IEGAD V FLG L S AAG VLT P EMVK S MA DN P I I F ALANP D PEI T P EE AK A VRPDAII A TGRSDYPNQVNNVL 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 323 CFP F IFRGALDVGAT A INEEMKLAAVRAIAELA HA E Q S EV VA S AYG D Q D LSFGPEYIIPKPFDPRLIVKIAPAVAKAAM E 402
Cdd:PRK07232 320 CFP Y IFRGALDVGAT T INEEMKLAAVRAIAELA RE E V S DE VA A AYG G Q K LSFGPEYIIPKPFDPRLIVKIAPAVAKAAM D 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 403 SGVATRPIAD F D V Y ID KL TE FVYKT N L F MKPIF SQ A R K A PKRVV LP EGEE A RVL H A T QE L V TL GLAKPILIGRP N VIE M R 482
Cdd:PRK07232 400 SGVATRPIAD M D A Y RE KL EA FVYKT G L V MKPIF AK A K K D PKRVV FA EGEE E RVL R A A QE V V DE GLAKPILIGRP E VIE A R 479
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 483 I Q KLGL QI KAGVDFEIVN N E S DPR FK EYW TE Y FQIMK R R GVT Q E Q A Q R ALISNP TVIGA I MV Q RG E ADAMICG TV G D YHE 562
Cdd:PRK07232 480 I K KLGL DL KAGVDFEIVN P E D DPR YE EYW QY Y YELLQ R K GVT P E D A R R LVRRDR TVIGA M MV A RG D ADAMICG LT G R YHE 559
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 563 H FSV V KN V F G Y R D GVHTA G AMNALLL PS GN T FIADTYVN DE P D AEELAEI T LMAAE T VRRFGIEPRVALLSHSNFGSSD C 642
Cdd:PRK07232 560 H LRP V RQ V I G L R P GVHTA A AMNALLL KG GN L FIADTYVN ED P T AEELAEI A LMAAE E VRRFGIEPRVALLSHSNFGSSD S 639
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 643 PS SS KMR Q A L EL V RERAP E L MI DGEMHGDAAL V E A IR N D RM P D S S LKG S AN I LVMPN M EAA R ISYNLL RV s SSE GVT V GP 722
Cdd:PRK07232 640 PS AR KMR E A V EL L RERAP D L EV DGEMHGDAAL N E E IR K D LY P F S R LKG P AN V LVMPN L EAA N ISYNLL KE - LGG GVT I GP 718
730 740 750
....*....|....*....|....*....|....
gi 16130388 723 V L M G V AKPVH V LTP I A S VRRIVNM V ALAVV E AQT 756
Cdd:PRK07232 719 I L L G M AKPVH I LTP S A T VRRIVNM T ALAVV D AQT 752
Name
Accession
Description
Interval
E-value
PRK07232
PRK07232 bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
3-756
0e+00
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
Pssm-ID: 235976 [Multi-domain]
Cd Length: 752
Bit Score: 1534.27
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 3 D QLKQ S ALD F H E FP V PGKI Q V S PTKPLATQRDL A LAYSPGVAAPCLEI E KDP LK AYKYTARGNLVAVISNGTAVLGLGNI 82
Cdd:PRK07232 1 E QLKQ A ALD Y H R FP R PGKI E V T PTKPLATQRDL S LAYSPGVAAPCLEI A KDP AD AYKYTARGNLVAVISNGTAVLGLGNI 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 83 GALA G KPVMEGKGVLFKKFAGIDVFDIEVDE L DPDKFIE V VAALEPTFGGINLEDIKAPECFYIE Q KLRERM N IPVFHDD 162
Cdd:PRK07232 81 GALA S KPVMEGKGVLFKKFAGIDVFDIEVDE E DPDKFIE A VAALEPTFGGINLEDIKAPECFYIE E KLRERM D IPVFHDD 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 QHGTAIIS T AA I LN G L RV V E K N I S DV RM VVSGAGAAAIAC M NLLVALG LQ K H NI V VCDSKGVIY Q GR EPN M A E T KAAYAV 242
Cdd:PRK07232 161 QHGTAIIS A AA L LN A L EL V G K K I E DV KI VVSGAGAAAIAC L NLLVALG AK K E NI I VCDSKGVIY K GR TEG M D E W KAAYAV 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 243 v D DGK RTL DDV IEGAD I FLG C S GPK VLT Q EMVK K MA RA P M I L ALANP E PEI L P PL AK E VRPDAII C TGRSDYPNQVNNVL 322
Cdd:PRK07232 241 - D TDA RTL AEA IEGAD V FLG L S AAG VLT P EMVK S MA DN P I I F ALANP D PEI T P EE AK A VRPDAII A TGRSDYPNQVNNVL 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 323 CFP F IFRGALDVGAT A INEEMKLAAVRAIAELA HA E Q S EV VA S AYG D Q D LSFGPEYIIPKPFDPRLIVKIAPAVAKAAM E 402
Cdd:PRK07232 320 CFP Y IFRGALDVGAT T INEEMKLAAVRAIAELA RE E V S DE VA A AYG G Q K LSFGPEYIIPKPFDPRLIVKIAPAVAKAAM D 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 403 SGVATRPIAD F D V Y ID KL TE FVYKT N L F MKPIF SQ A R K A PKRVV LP EGEE A RVL H A T QE L V TL GLAKPILIGRP N VIE M R 482
Cdd:PRK07232 400 SGVATRPIAD M D A Y RE KL EA FVYKT G L V MKPIF AK A K K D PKRVV FA EGEE E RVL R A A QE V V DE GLAKPILIGRP E VIE A R 479
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 483 I Q KLGL QI KAGVDFEIVN N E S DPR FK EYW TE Y FQIMK R R GVT Q E Q A Q R ALISNP TVIGA I MV Q RG E ADAMICG TV G D YHE 562
Cdd:PRK07232 480 I K KLGL DL KAGVDFEIVN P E D DPR YE EYW QY Y YELLQ R K GVT P E D A R R LVRRDR TVIGA M MV A RG D ADAMICG LT G R YHE 559
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 563 H FSV V KN V F G Y R D GVHTA G AMNALLL PS GN T FIADTYVN DE P D AEELAEI T LMAAE T VRRFGIEPRVALLSHSNFGSSD C 642
Cdd:PRK07232 560 H LRP V RQ V I G L R P GVHTA A AMNALLL KG GN L FIADTYVN ED P T AEELAEI A LMAAE E VRRFGIEPRVALLSHSNFGSSD S 639
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 643 PS SS KMR Q A L EL V RERAP E L MI DGEMHGDAAL V E A IR N D RM P D S S LKG S AN I LVMPN M EAA R ISYNLL RV s SSE GVT V GP 722
Cdd:PRK07232 640 PS AR KMR E A V EL L RERAP D L EV DGEMHGDAAL N E E IR K D LY P F S R LKG P AN V LVMPN L EAA N ISYNLL KE - LGG GVT I GP 718
730 740 750
....*....|....*....|....*....|....
gi 16130388 723 V L M G V AKPVH V LTP I A S VRRIVNM V ALAVV E AQT 756
Cdd:PRK07232 719 I L L G M AKPVH I LTP S A T VRRIVNM T ALAVV D AQT 752
SfcA
COG0281 Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
5-424
0e+00
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440050 [Multi-domain]
Cd Length: 414
Bit Score: 719.10
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 5 L K Q S AL DF H EFPVP GKI Q V S PT K PL A TQ R DL A LAY S PGVA AP CLEI EK DP LK AY K YTA R GNLVAV ISN GTAVLGLG N IG A 84
Cdd:COG0281 9 L E Q E AL EY H RIYDR GKI L V Y PT V PL H TQ E DL S LAY T PGVA EA CLEI AE DP RL AY G YTA K GNLVAV VTD GTAVLGLG D IG P 88
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 85 LAG K PVMEGK G VLFK K FAGID V F D I EV D EL DPD K F I E V V A ALEPTFGGINLEDIKAP E CF Y IE QK LRE RMN IPVFHDDQH 164
Cdd:COG0281 89 LAG M PVMEGK A VLFK A FAGID A F P I CL D TN DPD E F V E A V K ALEPTFGGINLEDIKAP N CF E IE ER LRE ELD IPVFHDDQH 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 165 GTAI IST AA I LN G L RV V E K NIS D VRM V VS GAGAA A IA CMN LLVA L GL QKH NI VVC DSKG VI Y Q GR e PNMAET K AAY A VV - 243
Cdd:COG0281 169 GTAI VVL AA L LN A L KL V G K KLE D QKI V IN GAGAA G IA IAR LLVA A GL SEE NI IMV DSKG LL Y E GR - TDLNPY K REF A RD t 247
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 244 -- DDG K R TL DDV I E GAD I F L G C S G P KVL T Q EMVK K MA RA P M I L ALANP E PEI L P PL AK EVRPD AI IC TGRSDYPNQVNNV 321
Cdd:COG0281 248 np RGL K G TL AEA I K GAD V F I G V S A P GAF T E EMVK S MA KR P I I F ALANP T PEI T P ED AK AWGDG AI VA TGRSDYPNQVNNV 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 322 L C FP F IFRGALDV G AT A I NE EMKLAA V RA I A E L AHA E Q sevvasaygdqdls F GP E YIIP K PFDPR LIVKI A P AVAKAA M 401
Cdd:COG0281 328 L I FP G IFRGALDV R AT R I TD EMKLAA A RA L A D L VDE E E -------------- L GP D YIIP S PFDPR VSPAV A A AVAKAA I 393
410 420
....*....|....*....|...
gi 16130388 402 ESGVA T RPI A df DV Y IDK L TEFV 424
Cdd:COG0281 394 ESGVA R RPI D -- ED Y REA L EARM 414
Malic_M
smart00919 Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
163-401
1.78e-117
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.
Pssm-ID: 214912
Cd Length: 231
Bit Score: 353.26
E-value: 1.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 Q H GTAI IST A AI LN G L RVVE K NIS D V R M VV S GAGAA A I ACMN LLVA L G LQKH NI VVC DSKG VIYQ GRE P N MAET K AAY A V 242
Cdd:smart00919 1 Q Q GTAI VVL A GL LN A L KITG K KLE D Q R I VV N GAGAA G I GIAK LLVA A G VKRK NI WLV DSKG LLTK GRE D N LNPY K KPF A R 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 243 VDDGKR -- TL DDVIE GAD IFL G C SGP K - VL T Q EMVK K MA RA P M I L AL A NP E PEI L P PL A KEV R P - D AI IC TGRSDYPNQV 318
Cdd:smart00919 81 KTNERE tg TL EEAVK GAD VLI G V SGP G g AF T E EMVK S MA ER P I I F AL S NP T PEI E P TA A DAY R W t A AI VA TGRSDYPNQV 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 319 NNVL C FP F IF R GALDV G A TA I NE EMKLAA VR A I A E lahaeqsevvas A YGDQDLSF GP E YIIP K PFD P R LIVKI A P AVAK 398
Cdd:smart00919 161 NNVL I FP G IF L GALDV R A RR I TD EMKLAA AE A L A D ------------ A VPVSEEEL GP G YIIP S PFD R R VSARV A V AVAK 228
...
gi 16130388 399 AA M 401
Cdd:smart00919 229 AA I 231
NAD_bind_2_malic_enz
cd05311 NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
163-400
5.49e-116
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133453 [Multi-domain]
Cd Length: 226
Bit Score: 349.26
E-value: 5.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 QHGTAI IST A AI LN G L RV V E K N I SD V RM V VS GAGAA A IA CMN LL V A L G LQKH NIVV C DSKGVIY Q GRE ---- P NMA E TKA 238
Cdd:cd05311 1 QHGTAI VTL A GL LN A L KL V G K K I EE V KI V IN GAGAA G IA IAR LL L A A G AKPE NIVV V DSKGVIY E GRE ddln P DKN E IAK 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 239 AYAVVDD G K r TL DDVIE GAD I F L G C S G P K V LTQ EM V KKMA RA P MIL ALANP E PEI L P PL AKE VRP D a I IC TGRSD Y PNQV 318
Cdd:cd05311 81 ETNPEKT G G - TL KEALK GAD V F I G V S R P G V VKK EM I KKMA KD P IVF ALANP V PEI W P EE AKE AGA D - I VA TGRSD F PNQV 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 319 NNVL C FP F IFRGALDV G AT A I N EEMKLAA VR AIA E LA HA E QS evvasaygdqdlsf G P EYIIP K PFDPR LIVKI A P AVAK 398
Cdd:cd05311 159 NNVL G FP G IFRGALDV R AT K I T EEMKLAA AE AIA D LA EE E VL -------------- G E EYIIP T PFDPR VVPRV A T AVAK 224
..
gi 16130388 399 AA 400
Cdd:cd05311 225 AA 226
PTA_PTB
pfam01515 Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
430-751
7.81e-114
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.
Pssm-ID: 396207 [Multi-domain]
Cd Length: 318
Bit Score: 346.99
E-value: 7.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 430 F MKP IF SQ A R KA P KR V V L PEGE EA RVL H A T Q E L VTL G L A K PILIG rp NV IE MRIQK LGL QIKAGV d F EIV NN E SD PR FK E 509
Cdd:pfam01515 1 F LER IF ER A K KA K KR I V F PEGE DE RVL K A A Q K L LQQ G I A D PILIG -- DE IE IKAKA LGL DLDLDG - I EIV DP E TS PR LE E 77
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 510 Y WTE Y FQIM KR R G V T Q E Q A QR a LISN P TVIG A IM V QR GEAD A M IC G T V GDYHEHFSVVKNVF G YRD GV H T AGAMNAL LLP 589
Cdd:pfam01515 78 Y ADF Y YELR KR K G M T P E I A RE - IVRD P NYFA A ML V KL GEAD G M VS G A V NTTADTLRPALQII G TKP GV K T VSSVFIM LLP 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 590 S G NT F I AD TY VN DE P D AEELAEI T LM A A E T VR RFG - IEPRVALLS H S N FGS SDCPSSS K M R Q A LEL VRERAP E L MI DGE M 668
Cdd:pfam01515 157 D G LL F F AD CA VN PN P T AEELAEI A LM S A K T AK RFG i IEPRVALLS Y S T FGS GKGEDVE K V R E A TKI VRERAP D L VV DGE L 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 669 HG DAALVE AIRNDRM PDS SLK G S AN IL V M P NM EA AR I S Y NLL - R VSSS E gv TV GP V L M G V AKPV HV L TPI ASV RR IVN MV 747
Cdd:pfam01515 237 QF DAALVE EVAAQKA PDS PVA G K AN VF V F P DL EA GN I G Y KIA q R LGGA E -- AI GP I L Q G L AKPV ND L SRG ASV ED IVN TA 314
....
gi 16130388 748 A LAV 751
Cdd:pfam01515 315 A ITA 318
Name
Accession
Description
Interval
E-value
PRK07232
PRK07232 bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
3-756
0e+00
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
Pssm-ID: 235976 [Multi-domain]
Cd Length: 752
Bit Score: 1534.27
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 3 D QLKQ S ALD F H E FP V PGKI Q V S PTKPLATQRDL A LAYSPGVAAPCLEI E KDP LK AYKYTARGNLVAVISNGTAVLGLGNI 82
Cdd:PRK07232 1 E QLKQ A ALD Y H R FP R PGKI E V T PTKPLATQRDL S LAYSPGVAAPCLEI A KDP AD AYKYTARGNLVAVISNGTAVLGLGNI 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 83 GALA G KPVMEGKGVLFKKFAGIDVFDIEVDE L DPDKFIE V VAALEPTFGGINLEDIKAPECFYIE Q KLRERM N IPVFHDD 162
Cdd:PRK07232 81 GALA S KPVMEGKGVLFKKFAGIDVFDIEVDE E DPDKFIE A VAALEPTFGGINLEDIKAPECFYIE E KLRERM D IPVFHDD 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 QHGTAIIS T AA I LN G L RV V E K N I S DV RM VVSGAGAAAIAC M NLLVALG LQ K H NI V VCDSKGVIY Q GR EPN M A E T KAAYAV 242
Cdd:PRK07232 161 QHGTAIIS A AA L LN A L EL V G K K I E DV KI VVSGAGAAAIAC L NLLVALG AK K E NI I VCDSKGVIY K GR TEG M D E W KAAYAV 240
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 243 v D DGK RTL DDV IEGAD I FLG C S GPK VLT Q EMVK K MA RA P M I L ALANP E PEI L P PL AK E VRPDAII C TGRSDYPNQVNNVL 322
Cdd:PRK07232 241 - D TDA RTL AEA IEGAD V FLG L S AAG VLT P EMVK S MA DN P I I F ALANP D PEI T P EE AK A VRPDAII A TGRSDYPNQVNNVL 319
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 323 CFP F IFRGALDVGAT A INEEMKLAAVRAIAELA HA E Q S EV VA S AYG D Q D LSFGPEYIIPKPFDPRLIVKIAPAVAKAAM E 402
Cdd:PRK07232 320 CFP Y IFRGALDVGAT T INEEMKLAAVRAIAELA RE E V S DE VA A AYG G Q K LSFGPEYIIPKPFDPRLIVKIAPAVAKAAM D 399
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 403 SGVATRPIAD F D V Y ID KL TE FVYKT N L F MKPIF SQ A R K A PKRVV LP EGEE A RVL H A T QE L V TL GLAKPILIGRP N VIE M R 482
Cdd:PRK07232 400 SGVATRPIAD M D A Y RE KL EA FVYKT G L V MKPIF AK A K K D PKRVV FA EGEE E RVL R A A QE V V DE GLAKPILIGRP E VIE A R 479
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 483 I Q KLGL QI KAGVDFEIVN N E S DPR FK EYW TE Y FQIMK R R GVT Q E Q A Q R ALISNP TVIGA I MV Q RG E ADAMICG TV G D YHE 562
Cdd:PRK07232 480 I K KLGL DL KAGVDFEIVN P E D DPR YE EYW QY Y YELLQ R K GVT P E D A R R LVRRDR TVIGA M MV A RG D ADAMICG LT G R YHE 559
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 563 H FSV V KN V F G Y R D GVHTA G AMNALLL PS GN T FIADTYVN DE P D AEELAEI T LMAAE T VRRFGIEPRVALLSHSNFGSSD C 642
Cdd:PRK07232 560 H LRP V RQ V I G L R P GVHTA A AMNALLL KG GN L FIADTYVN ED P T AEELAEI A LMAAE E VRRFGIEPRVALLSHSNFGSSD S 639
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 643 PS SS KMR Q A L EL V RERAP E L MI DGEMHGDAAL V E A IR N D RM P D S S LKG S AN I LVMPN M EAA R ISYNLL RV s SSE GVT V GP 722
Cdd:PRK07232 640 PS AR KMR E A V EL L RERAP D L EV DGEMHGDAAL N E E IR K D LY P F S R LKG P AN V LVMPN L EAA N ISYNLL KE - LGG GVT I GP 718
730 740 750
....*....|....*....|....*....|....
gi 16130388 723 V L M G V AKPVH V LTP I A S VRRIVNM V ALAVV E AQT 756
Cdd:PRK07232 719 I L L G M AKPVH I LTP S A T VRRIVNM T ALAVV D AQT 752
PRK12862
PRK12862 malic enzyme; Reviewed
1-755
0e+00
malic enzyme; Reviewed
Pssm-ID: 183799 [Multi-domain]
Cd Length: 763
Bit Score: 1399.63
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 1 MDDQ L KQS ALD F H E FP V PGKI QVS PTKPLA T QRDLALAYSPGVAAPCLEI EK DP LK A YK YT A RGNLVAV I SNGTAVLGLG 80
Cdd:PRK12862 7 AKAE L REA ALD Y H R FP T PGKI EIA PTKPLA N QRDLALAYSPGVAAPCLEI AA DP AN A AR YT S RGNLVAV V SNGTAVLGLG 86
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 81 NIG A LA G KPVMEGK G VLFKKFAGIDVFDIE V DE L DPDK FI E V VAALEPTFGGINLEDIKAPECFYIE QK LRERM N IPVFH 160
Cdd:PRK12862 87 NIG P LA S KPVMEGK A VLFKKFAGIDVFDIE L DE S DPDK LV E I VAALEPTFGGINLEDIKAPECFYIE RE LRERM K IPVFH 166
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 161 DDQHGTAII ST AA I LNGL RV V E K N I S DV RM V V SGAGAAA I AC MN LLV A LG LQKH NI V V C D S KGV I Y Q GR EPN M AET KA A Y 240
Cdd:PRK12862 167 DDQHGTAII VA AA L LNGL KL V G K D I E DV KL V A SGAGAAA L AC LD LLV S LG VKRE NI W V T D I KGV V Y E GR TEL M DPW KA R Y 246
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 241 A VVD D g K RTL DD VIEGAD I FLG C S GPK VL TQ EMVKKMA RA P M I L ALANP E PEILP PL A KE VRPDAII C TGRSDYPNQVNN 320
Cdd:PRK12862 247 A QKT D - A RTL AE VIEGAD V FLG L S AAG VL KP EMVKKMA PR P L I F ALANP T PEILP EE A RA VRPDAII A TGRSDYPNQVNN 325
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 321 VLCFP F IFRGALDVGAT A INEEMK L AAVRAIAELA HA EQS E VVA S AYG DQ DLSFGP E Y I IPKPFDPRLI V KIAPAVA K AA 400
Cdd:PRK12862 326 VLCFP Y IFRGALDVGAT T INEEMK I AAVRAIAELA RE EQS D VVA A AYG GE DLSFGP D Y L IPKPFDPRLI L KIAPAVA Q AA 405
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 401 M E SGVATRPI A D F D V Y IDK L TE FVY KTN L F MKP I F SQ A RK APKRVV LP EGE EA RVL H A T Q EL V TL GLAKPILIGRP N VIE 480
Cdd:PRK12862 406 M D SGVATRPI E D M D A Y REQ L NQ FVY HSG L I MKP V F AA A KA APKRVV FA EGE DE RVL R A A Q VV V DE GLAKPILIGRP A VIE 485
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 481 M RI QKL GL QIKA GVDFEIVN N E S DPR FKE YW TE Y FQI M K R R GVT Q E Q A Q R ALISNP T V IGA I MV Q RGEADAMICGT V G D Y 560
Cdd:PRK12862 486 A RI ERA GL RLRP GVDFEIVN P E D DPR YRD YW DT Y HAL M G R K GVT P E M A R R EVRRRT T L IGA M MV K RGEADAMICGT E G R Y 565
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 561 HE H FSV V KN V F G Y R D GV HTAG AM NA L L LP SGNT F I ADT Y VN DE P D AEELAEIT LM AAE T VRRFGIEP R VALLSHSNFGSS 640
Cdd:PRK12862 566 ER H LEF V LQ V I G K R P GV RVYA AM SL L I LP GRTL F L ADT H VN ED P T AEELAEIT IL AAE E VRRFGIEP K VALLSHSNFGSS 645
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 641 D C PS SS KMR Q ALE LV RERAP E L MI DGEMHGDAAL V E AI R NDRM PDS S L K G S AN I LV M PN ME AA R I S YNLL RVSSSE G VT V 720
Cdd:PRK12862 646 D S PS AR KMR E ALE IL RERAP D L EV DGEMHGDAAL D E EL R DRIF PDS R L E G E AN L LV F PN LD AA N I A YNLL KTAAGN G LA V 725
730 740 750
....*....|....*....|....*....|....*
gi 16130388 721 GP V L M G V AKPVH V LTP I A S VRRIVNM V ALAV VE A Q 755
Cdd:PRK12862 726 GP I L L G A AKPVH I LTP S A T VRRIVNM T ALAV AD A N 760
PRK12861
PRK12861 malic enzyme; Reviewed
1-754
0e+00
malic enzyme; Reviewed
Pssm-ID: 183798 [Multi-domain]
Cd Length: 764
Bit Score: 1066.81
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 1 MDDQLK Q S ALD F HEFP V PGKI Q V SPT KPL A TQRDLALAY S PGVA AP C L EI EK DPL K A YKY T A RGNLV A VI S NGTAVLGLG 80
Cdd:PRK12861 3 QTETQR Q A ALD Y HEFP T PGKI S V VAS KPL V TQRDLALAY T PGVA SA C E EI AA DPL N A FRF T S RGNLV G VI T NGTAVLGLG 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 81 NIGALA G KPVMEGK G VLFKKFAGIDVFDIE VD E L DPDK FIEVV A A LEPTFGGINLEDIKAPECF YI E Q KLRERM N IPVFH 160
Cdd:PRK12861 83 NIGALA S KPVMEGK A VLFKKFAGIDVFDIE IN E T DPDK LVDII A G LEPTFGGINLEDIKAPECF TV E R KLRERM K IPVFH 162
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 161 DDQHGTAI IST AA IL NGL R VV E K N I SD V RM V V SGAGAAA I AC MN LLV A LGL QKH NI V V C D SK GV I Y Q GR EPN M AET K AAY 240
Cdd:PRK12861 163 DDQHGTAI TVS AA FI NGL K VV G K S I KE V KV V T SGAGAAA L AC LD LLV D LGL PVE NI W V T D IE GV V Y R GR TTL M DPD K ERF 242
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 241 A VVD D G k RTL DD VI E GAD I FLG C S GPK VL TQ EM V K K MA RA P M ILALANP E PEI L P P LA KEV R P D AI I C TGRSDYPNQVNN 320
Cdd:PRK12861 243 A QET D A - RTL AE VI G GAD V FLG L S AGG VL KA EM L K A MA AR P L ILALANP T PEI F P E LA HAT R D D VV I A TGRSDYPNQVNN 321
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 321 VLCFP F IFRGALDVGAT A I NE EM KL AAV R AIA E LA HA EQ SE VVA S AYG DQ D L SFGP E Y I IPKPFDPRLIV K IAPAVAKAA 400
Cdd:PRK12861 322 VLCFP Y IFRGALDVGAT T I TR EM EI AAV H AIA G LA EE EQ ND VVA A AYG AY D V SFGP Q Y L IPKPFDPRLIV R IAPAVAKAA 401
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 401 ME S GVATRPIAD F D V Y IDK L TE FVY KTNL FMKP I F SQ AR K ----- APK R V V LP EGE EA RVL H A T Q EL V TLG LA K PIL I GR 475
Cdd:PRK12861 402 ME G GVATRPIAD L D A Y VEQ L QQ FVY HSGA FMKP L F AA AR Q lvrdg GKA R I V FT EGE DE RVL R A V Q VI V DEK LA R PIL V GR 481
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 476 P N V IEM RI QKL GL QIKA G V D F E IV N N E S D P RF KE YWT E Y FQIMK R R G VTQ E Q A QRALISNP T V IGA I MV QR G E AD A MICG 555
Cdd:PRK12861 482 P E V LLA RI ERF GL RLRL G Q D V E VT N P E Y D E RF PQ YWT T Y WELRC R D G ISK E M A RVEMRRRL T L IGA M MV RL G D AD G MICG 561
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 556 TVG D YH E H FSV V KN V F G YRD G VH T AG AMN A LLL PSGNTFIA DT Y VND E PDAE EL AE I T LM AA ETVRRFGIE P R VALLS H S 635
Cdd:PRK12861 562 TVG E YH N H LRF V DE V I G RKP G AS T YA AMN I LLL DQRTVALV DT H VND N PDAE QI AE F T IA AA RQMEWLNLT P K VALLS R S 641
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 636 NFGS SDCP S SS KMR Q ALE L VRE R AP E L MI DGEMHGD A AL V E AI R NDRM P D S S LKG S AN I LV M PN ME A AR I S YNLL RVSSS 715
Cdd:PRK12861 642 NFGS GSAA S GV KMR R ALE I VRE Q AP D L EA DGEMHGD C AL D E GL R ARLL P M S P LKG A AN L LV C PN VD A GN I A YNLL KTEAG 721
730 740 750
....*....|....*....|....*....|....*....
gi 16130388 716 EG V T VGP V L M GV AK PV HV LT PI A S VRRIVNM V AL A V V EA 754
Cdd:PRK12861 722 SN V A VGP F L L GV NA PV NI LT SS A T VRRIVNM A AL T V I EA 760
SfcA
COG0281 Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
5-424
0e+00
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440050 [Multi-domain]
Cd Length: 414
Bit Score: 719.10
E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 5 L K Q S AL DF H EFPVP GKI Q V S PT K PL A TQ R DL A LAY S PGVA AP CLEI EK DP LK AY K YTA R GNLVAV ISN GTAVLGLG N IG A 84
Cdd:COG0281 9 L E Q E AL EY H RIYDR GKI L V Y PT V PL H TQ E DL S LAY T PGVA EA CLEI AE DP RL AY G YTA K GNLVAV VTD GTAVLGLG D IG P 88
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 85 LAG K PVMEGK G VLFK K FAGID V F D I EV D EL DPD K F I E V V A ALEPTFGGINLEDIKAP E CF Y IE QK LRE RMN IPVFHDDQH 164
Cdd:COG0281 89 LAG M PVMEGK A VLFK A FAGID A F P I CL D TN DPD E F V E A V K ALEPTFGGINLEDIKAP N CF E IE ER LRE ELD IPVFHDDQH 168
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 165 GTAI IST AA I LN G L RV V E K NIS D VRM V VS GAGAA A IA CMN LLVA L GL QKH NI VVC DSKG VI Y Q GR e PNMAET K AAY A VV - 243
Cdd:COG0281 169 GTAI VVL AA L LN A L KL V G K KLE D QKI V IN GAGAA G IA IAR LLVA A GL SEE NI IMV DSKG LL Y E GR - TDLNPY K REF A RD t 247
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 244 -- DDG K R TL DDV I E GAD I F L G C S G P KVL T Q EMVK K MA RA P M I L ALANP E PEI L P PL AK EVRPD AI IC TGRSDYPNQVNNV 321
Cdd:COG0281 248 np RGL K G TL AEA I K GAD V F I G V S A P GAF T E EMVK S MA KR P I I F ALANP T PEI T P ED AK AWGDG AI VA TGRSDYPNQVNNV 327
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 322 L C FP F IFRGALDV G AT A I NE EMKLAA V RA I A E L AHA E Q sevvasaygdqdls F GP E YIIP K PFDPR LIVKI A P AVAKAA M 401
Cdd:COG0281 328 L I FP G IFRGALDV R AT R I TD EMKLAA A RA L A D L VDE E E -------------- L GP D YIIP S PFDPR VSPAV A A AVAKAA I 393
410 420
....*....|....*....|...
gi 16130388 402 ESGVA T RPI A df DV Y IDK L TEFV 424
Cdd:COG0281 394 ESGVA R RPI D -- ED Y REA L EARM 414
Pta
COG0280 Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ...
430-753
2.38e-148
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production and conversion];
Pssm-ID: 440049 [Multi-domain]
Cd Length: 320
Bit Score: 436.04
E-value: 2.38e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 430 F MK P IFSQ A RK APKR V V LP EGE EA RVL H A T QE LVTL GLA K PIL I GRP NV IE M R IQK LGL QIK agv D FEI VNN E SD PR FK E 509
Cdd:COG0280 2 F FR P LIER A KA APKR I V FA EGE DE RVL R A A QE ALDE GLA E PIL V GRP EK IE A R AEE LGL DLS --- G FEI IDP E DS PR YE E 78
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 510 Y WTE Y FQIM KR R GVT Q E Q A QR a L ISNPTVIG A I MV QR GEAD AMIC G T VG DYHEHFSV V KNVF G Y R D GV HTAGAMNALL LP 589
Cdd:COG0280 79 Y AEA Y YELR KR K GVT P E E A RE - L VRDAAYFA A M MV RL GEAD GLVK G A VG TTADLLRP V LQII G L R P GV KRVSHVFLME LP 157
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 590 SGNT FI A DT Y VN DE P D AE E LA E I TLM AA E T V R R FGIEP R VALLS H S N FGS SDC PS SS K M R Q A LELV R ERA P E L MI DGE MH 669
Cdd:COG0280 158 DRLL FI T DT A VN ID P T AE Q LA D I AIN AA D T A R A FGIEP K VALLS A S E FGS PKG PS TD K V R E A TKMA R GQI P D L EV DGE LQ 237
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 670 G DAAL VEAIRNDRM PDS SLK G S AN I LV M P NM EA AR I S Y N LL RV s SSEGVTV GP V L M G V AKPVH V L TPIA SVR R IVN MV AL 749
Cdd:COG0280 238 F DAAL SPEAAKRKG PDS PVA G D AN V LV F P DL EA GN I L Y K LL QR - LAGAEAI GP I L L G L AKPVH L L SRGD SVR D IVN SI AL 316
....
gi 16130388 750 A V V E 753
Cdd:COG0280 317 A A V Q 320
Malic_M
smart00919 Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
163-401
1.78e-117
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.
Pssm-ID: 214912
Cd Length: 231
Bit Score: 353.26
E-value: 1.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 Q H GTAI IST A AI LN G L RVVE K NIS D V R M VV S GAGAA A I ACMN LLVA L G LQKH NI VVC DSKG VIYQ GRE P N MAET K AAY A V 242
Cdd:smart00919 1 Q Q GTAI VVL A GL LN A L KITG K KLE D Q R I VV N GAGAA G I GIAK LLVA A G VKRK NI WLV DSKG LLTK GRE D N LNPY K KPF A R 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 243 VDDGKR -- TL DDVIE GAD IFL G C SGP K - VL T Q EMVK K MA RA P M I L AL A NP E PEI L P PL A KEV R P - D AI IC TGRSDYPNQV 318
Cdd:smart00919 81 KTNERE tg TL EEAVK GAD VLI G V SGP G g AF T E EMVK S MA ER P I I F AL S NP T PEI E P TA A DAY R W t A AI VA TGRSDYPNQV 160
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 319 NNVL C FP F IF R GALDV G A TA I NE EMKLAA VR A I A E lahaeqsevvas A YGDQDLSF GP E YIIP K PFD P R LIVKI A P AVAK 398
Cdd:smart00919 161 NNVL I FP G IF L GALDV R A RR I TD EMKLAA AE A L A D ------------ A VPVSEEEL GP G YIIP S PFD R R VSARV A V AVAK 228
...
gi 16130388 399 AA M 401
Cdd:smart00919 229 AA I 231
NAD_bind_2_malic_enz
cd05311 NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
163-400
5.49e-116
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133453 [Multi-domain]
Cd Length: 226
Bit Score: 349.26
E-value: 5.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 QHGTAI IST A AI LN G L RV V E K N I SD V RM V VS GAGAA A IA CMN LL V A L G LQKH NIVV C DSKGVIY Q GRE ---- P NMA E TKA 238
Cdd:cd05311 1 QHGTAI VTL A GL LN A L KL V G K K I EE V KI V IN GAGAA G IA IAR LL L A A G AKPE NIVV V DSKGVIY E GRE ddln P DKN E IAK 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 239 AYAVVDD G K r TL DDVIE GAD I F L G C S G P K V LTQ EM V KKMA RA P MIL ALANP E PEI L P PL AKE VRP D a I IC TGRSD Y PNQV 318
Cdd:cd05311 81 ETNPEKT G G - TL KEALK GAD V F I G V S R P G V VKK EM I KKMA KD P IVF ALANP V PEI W P EE AKE AGA D - I VA TGRSD F PNQV 158
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 319 NNVL C FP F IFRGALDV G AT A I N EEMKLAA VR AIA E LA HA E QS evvasaygdqdlsf G P EYIIP K PFDPR LIVKI A P AVAK 398
Cdd:cd05311 159 NNVL G FP G IFRGALDV R AT K I T EEMKLAA AE AIA D LA EE E VL -------------- G E EYIIP T PFDPR VVPRV A T AVAK 224
..
gi 16130388 399 AA 400
Cdd:cd05311 225 AA 226
PTA_PTB
pfam01515 Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
430-751
7.81e-114
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.
Pssm-ID: 396207 [Multi-domain]
Cd Length: 318
Bit Score: 346.99
E-value: 7.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 430 F MKP IF SQ A R KA P KR V V L PEGE EA RVL H A T Q E L VTL G L A K PILIG rp NV IE MRIQK LGL QIKAGV d F EIV NN E SD PR FK E 509
Cdd:pfam01515 1 F LER IF ER A K KA K KR I V F PEGE DE RVL K A A Q K L LQQ G I A D PILIG -- DE IE IKAKA LGL DLDLDG - I EIV DP E TS PR LE E 77
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 510 Y WTE Y FQIM KR R G V T Q E Q A QR a LISN P TVIG A IM V QR GEAD A M IC G T V GDYHEHFSVVKNVF G YRD GV H T AGAMNAL LLP 589
Cdd:pfam01515 78 Y ADF Y YELR KR K G M T P E I A RE - IVRD P NYFA A ML V KL GEAD G M VS G A V NTTADTLRPALQII G TKP GV K T VSSVFIM LLP 156
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 590 S G NT F I AD TY VN DE P D AEELAEI T LM A A E T VR RFG - IEPRVALLS H S N FGS SDCPSSS K M R Q A LEL VRERAP E L MI DGE M 668
Cdd:pfam01515 157 D G LL F F AD CA VN PN P T AEELAEI A LM S A K T AK RFG i IEPRVALLS Y S T FGS GKGEDVE K V R E A TKI VRERAP D L VV DGE L 236
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 669 HG DAALVE AIRNDRM PDS SLK G S AN IL V M P NM EA AR I S Y NLL - R VSSS E gv TV GP V L M G V AKPV HV L TPI ASV RR IVN MV 747
Cdd:pfam01515 237 QF DAALVE EVAAQKA PDS PVA G K AN VF V F P DL EA GN I G Y KIA q R LGGA E -- AI GP I L Q G L AKPV ND L SRG ASV ED IVN TA 314
....
gi 16130388 748 A LAV 751
Cdd:pfam01515 315 A ITA 318
eutD
PRK09653 phosphotransacetylase;
430-757
8.66e-73
phosphotransacetylase;
Pssm-ID: 236609 [Multi-domain]
Cd Length: 324
Bit Score: 239.75
E-value: 8.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 430 FMKPIFSQ A RKAP K RV VLPEGE EA RVL H A TQE L VTL GL AK PIL I G R P NV I EMRIQK LGL QIK agv DF EI VNN E SD P RFK E 509
Cdd:PRK09653 3 LFESLKEK A KGKK K KI VLPEGE DE RVL K A AKR L QKE GL VE PIL L G N P EE I RAKAKE LGL DLD --- GV EI IDP E TY P LLE E 79
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 510 YWTEYFQIM K RR G VT q E Q A QRA L i SN P TVI G AIM V QR G E AD A M IC G --- TVG D yhehfs VVK --- NVFGYRD GV H T - AGA 582
Cdd:PRK09653 80 FAEAFVELR K GK G TE - E D A AEL L - KD P NYF G TML V KL G K AD G M VS G aih STA D ------ TLR pal QIIKTKP GV K T v SSV 151
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 583 M na LLLPSGNTF I - AD TY VN DE P D AE E LAEI TLMA AET VRR FGI E P R VA L LS H S NF GS SDC P SSS K MRQ A L E LVR E R AP E 661
Cdd:PRK09653 152 F -- IMVKGDERY I f AD CA VN PN P T AE Q LAEI AINS AET AKA FGI D P K VA M LS F S TK GS AKG P EVD K VQE A T E IAK E L AP D 229
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 662 L M IDGE MHG DAA L V EAIRNDRM P D S SLK G S AN IL V M P NM EA AR I S Y NLL - R VSSS E G vt VGP V L M G VA KPV HV L TPIA SV 740
Cdd:PRK09653 230 L K IDGE LQF DAA F V PEVAAKKA P G S PVA G K AN VF V F P SL EA GN I G Y KIA q R LGGF E A -- VGP I L Q G LN KPV ND L SRGC SV 307
330
....*....|....*..
gi 16130388 741 RR I V N MVALAVVE AQ TQ 757
Cdd:PRK09653 308 ED I Y N LALITAAQ AQ GE 324
PRK05632
PRK05632 phosphate acetyltransferase; Reviewed
437-755
7.92e-55
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain]
Cd Length: 684
Bit Score: 200.38
E-value: 7.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 437 Q AR K A P KR V VLPEG E E A R V L H A TQELVTL G L A KPI L I G R P NV I EMRIQKL G LQIK AG V df EI VN ne SDPRFKE Y WTEYFQ 516
Cdd:PRK05632 372 R AR A A K KR I VLPEG D E P R T L K A AAICLER G I A DCV L L G N P EE I RRVAAAQ G VDLP AG I -- EI ID -- PSEVRER Y VAPLVE 447
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 517 IM K RR G V T Q E Q A q R ALISNPTVI G AI M VQR GE A D AMIC G T V gdyhe H ------------------ F S V V KN VF gyrdgvh 578
Cdd:PRK05632 448 LR K HK G M T E E V A - R EQLEDNVYF G TM M LAL GE V D GLVS G A V ----- H ttantirpalqliktapg S S L V SS VF ------- 514
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 579 tag A M nal LLP SGNTFIA D TY VN DE P D AE E LAEI TLMA A ETVRR FGIEPRVA L LS H S N f G S S ------ D cpsss K M R Q A L 652
Cdd:PRK05632 515 --- F M --- LLP DQVLVYG D CA VN PD P T AE Q LAEI AIQS A DSAAA FGIEPRVA M LS Y S T - G T S gsgadv E ----- K V R E A T 582
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 653 E L V RER A P E L M IDG EMHG DAA LVEAIRNDRM P D S SLK G S A NILVM P NMEAARIS Y N ll R V SS S E G - V TV GP V L M G VA KPV 731
Cdd:PRK05632 583 R L A RER R P D L L IDG PLQY DAA VDPSVARSKA P N S PVA G R A TVFIF P DLNTGNTT Y K -- A V QR S A G a V SI GP M L Q G LR KPV 660
330 340
....*....|....*....|....
gi 16130388 732 HV L TPI A S V RR IVN MV A LAVVE AQ 755
Cdd:PRK05632 661 ND L SRG A L V DD IVN TI A ITAIQ AQ 684
malic
pfam00390 Malic enzyme, N-terminal domain;
18-151
8.55e-46
Malic enzyme, N-terminal domain;
Pssm-ID: 395314 [Multi-domain]
Cd Length: 182
Bit Score: 161.66
E-value: 8.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 18 P GK IQ V SPT K P L A T Q -- R DL ALA Y S P G V AAP C LE I EKDPLKAY - K YT AR GNL ---------------- V A V ISN G TAV LG 78
Cdd:pfam00390 1 Q GK NE V LFY K L L S T H ie E DL PIV Y T P T V GEA C QA I SEIYRRPR g L YT SI GNL gkikdilknwpeedvr V I V VTD G ERI LG 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 79 LG NI G A l AG K P V MEGK GV L FKK FAGID --- V FD I EV D E --------------------------- LDP D K F I E V V A AL E P 128
Cdd:pfam00390 81 LG DL G V - AG M P I MEGK LA L YTA FAGID psr V LP I VL D V gtnnekllndplylglrhkrvrgeeyd EFV D E F V E A V K AL F P 159
170 180
....*....|....*....|...
gi 16130388 129 T FGGI NL ED IK AP EC F Y I EQKL R 151
Cdd:pfam00390 160 P FGGI QF ED FG AP NA F E I LERY R 182
PTZ00317
PTZ00317 NADP-dependent malic enzyme; Provisional
67-359
4.39e-32
NADP-dependent malic enzyme; Provisional
Pssm-ID: 240357 [Multi-domain]
Cd Length: 559
Bit Score: 131.67
E-value: 4.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 67 V A VI SN G TAV LGLG NI GA l A G KPVME GK GV L FKKFA GI D ------- V F D IEVDEL ---- DP ------------------- 116
Cdd:PTZ00317 151 V I VI TD G SRI LGLG DL GA - N G MGISI GK LS L YVAGG GI N psrvlpv V L D VGTNNE klln DP lylglrekrldddeyyell 229
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 117 D K F I E V V AALE P T f GGINL ED IKAPE CF YIEQKLRER mn IPV F H DD QH GT AIIST A AI LN G L RVVEKNISDV R M V VS GAG 196
Cdd:PTZ00317 230 D E F M E A V SSRW P N - AVVQF ED FSNNH CF DLLERYQNK -- YRC F N DD IQ GT GAVIA A GF LN A L KLSGVPPEEQ R I V FF GAG 306
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 197 A AAI ACM N LLVA L ---- G LQ ---- KHNIVVC DSKG VIYQG R EPNM A ET K AAY A VV D ----- DGKR TL D DV IEGA -- DIF L 261
Cdd:PTZ00317 307 S AAI GVA N NIAD L aaey G VT reea LKSFYLV DSKG LVTTT R GDKL A KH K VPF A RT D isaed SSLK TL E DV VRFV kp TAL L 386
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 262 G C SG - PK V L T Q E M VK K MA RA --- P M I LA L A NP -- EP E ILPPL A - K EVRPD AI ICT G ---------- RSDY P N Q V NN VLC F 324
Cdd:PTZ00317 387 G L SG v GG V F T E E V VK T MA SN ver P I I FP L S NP ts KA E CTAED A y K WTNGR AI VAS G spfppvtlng KTIQ P S Q G NN LYV F 466
330 340 350
....*....|....*....|....*....|....*
gi 16130388 325 P FIFR G ALDVGATA I NE EM KL AA VRAI A E L AHA E Q 359
Cdd:PTZ00317 467 P GVGL G CAIAQPSY I PD EM LI AA AASL A T L VSE E D 501
PRK13529
PRK13529 oxaloacetate-decarboxylating malate dehydrogenase;
67-412
1.71e-31
oxaloacetate-decarboxylating malate dehydrogenase;
Pssm-ID: 237414 [Multi-domain]
Cd Length: 563
Bit Score: 130.25
E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 67 VA V ISN G TAV LG L G NI G ALA - G K P V me GK GV L FKKFA GID ------- V F D IEVD -- E L -- DP ------------------ 116
Cdd:PRK13529 149 LI V VTD G ERI LG I G DQ G IGG m G I P I -- GK LS L YTACG GID partlpv V L D VGTN ne Q L ln DP lylgwrhprirgeeydef 226
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 117 - D K F IEV V AALE P tfggi N L ---- ED IKAPECFY I EQKL R ER mn I PV F H DD QH GT AIIST A AI L NG L RVVEKNI SD V R M V 191
Cdd:PRK13529 227 v D E F VQA V KRRF P ----- N A llqf ED FAQKNARR I LERY R DE -- I CT F N DD IQ GT GAVTL A GL L AA L KITGEPL SD Q R I V 299
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 192 VS GAG A A AIACMNLL VA L ---- GL ----- Q K HNIV V c D SK G VIYQGR e P NMAETKAA YA --------- VVDDGKRT L DD V 253
Cdd:PRK13529 300 FL GAG S A GCGIADQI VA A mvre GL seeea R K RFFM V - D RQ G LLTDDM - P DLLDFQKP YA rkreeladw DTEGDVIS L LE V 377
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 254 IEGA -- DIFL G C SG - P KVL T Q E M VK K MA RA --- P M I LA L A NP epeil PPL A k E VR P D --------- A IIC TG -------- 310
Cdd:PRK13529 378 VRNV kp TVLI G V SG q P GAF T E E I VK E MA AH cer P I I FP L S NP ----- TSR A - E AT P E dliawtdgr A LVA TG spfapvey 451
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 311 -- RSDYPN Q V NN VLC FP FIFR G ALDV GA TAINEE M KL AA VR A I A ELAHAEQSE v VASAYGD ---- QDL S fgpeyiipkpf 384
Cdd:PRK13529 452 ng KTYPIG Q C NN AYI FP GLGL G VIAS GA RRVTDG M LM AA AH A L A DCVPLAKPG - EGALLPP vedi REV S ----------- 519
410 420
....*....|....*....|....*...
gi 16130388 385 dprli VK IA P AVAKAA M E S G V A TRPIAD 412
Cdd:PRK13529 520 ----- RA IA I AVAKAA I E E G L A RETSDE 542
PLN03129
PLN03129 NADP-dependent malic enzyme; Provisional
67-409
5.03e-31
NADP-dependent malic enzyme; Provisional
Pssm-ID: 215594 [Multi-domain]
Cd Length: 581
Bit Score: 128.88
E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 67 V A V ISN G TAV LGLG NI G ALA - G K PV me GK GV L FKKFA GI D --- V FDIEV D ------ E L -- DP --------------- D KF 119
Cdd:PLN03129 174 V I V VTD G ERI LGLG DL G VQG m G I PV -- GK LD L YTAAG GI R psa V LPVCI D vgtnne K L ln DP fyiglrqprltgeey D EL 251
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 120 I - E VVA A LEPTF G G --- INL ED IKAPEC F YIE Q KL R E rm NIPV F H DD QH GTA IIST A AI L NG LR VVEKNIS D V R MVVS GA 195
Cdd:PLN03129 252 V d E FME A VKQRW G P kvl VQF ED FANKNA F RLL Q RY R T -- THLC F N DD IQ GTA AVAL A GL L AA LR ATGGDLA D Q R ILFA GA 329
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 196 G A A AIACMN L L v AL GLQKH ---------- N I VVC DSKG VIYQG R EPNMAET K AAY A - VVDD G K r T L DDVIEGA -- DIFL G 262
Cdd:PLN03129 330 G E A GTGIAE L I - AL AMSRQ tgiseeeark R I WLV DSKG LVTKS R KDSLQPF K KPF A h DHEP G A - S L LEAVKAI kp TVLI G 407
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 263 C SG - PKVL T Q E MVKK MA --- RA P M I L AL A NP E -- P E ILPPL A - KEVRPD AI ICT ---------- G RSDY P N Q V NN VLC FP 325
Cdd:PLN03129 408 L SG v GGTF T K E VLEA MA sln ER P I I F AL S NP T sk A E CTAEE A y TWTGGR AI FAS gspfdpveyn G KTFH P G Q A NN AYI FP 487
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 326 F I FR GAL DV GA TAINEE M K LAA VR A I A ELAHA E qsevvasaygdq D L SF G pey I I PK PF DP - R L I - VKI A P AVA KA A M E S 403
Cdd:PLN03129 488 G I GL GAL LS GA IRVTDD M L LAA AE A L A AQVTE E ------------ E L AK G --- A I YP PF SR i R D I s AHV A A AVA AK A Y E E 552
....*.
gi 16130388 404 G V ATR P 409
Cdd:PLN03129 553 G L ATR L 558
NAD_bind_1_malic_enz
cd05312 NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
165-409
4.78e-29
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists of eukaryotic and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133454
Cd Length: 279
Bit Score: 117.26
E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 165 GTA IIST A AI L NG LR VVE K NI SD V R MVVS GAG A A A I ---- ACMNLL V AL GL QKH ---- N I VVC DSKG VIYQG R E p NMAET 236
Cdd:cd05312 3 GTA AVAL A GL L AA LR ITG K PL SD Q R ILFL GAG S A G I giad LIVSAM V RE GL SEE eark K I WLV DSKG LLTKD R K - DLTPF 81
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 237 K AAY A VV D D -- GKRT L DD V IE -- GADIFL G C SG - PKVL T Q E M V KK MA RA --- P M I L AL A N pepeilp P LA K - E VRPD --- 304
Cdd:cd05312 82 K KPF A RK D E ek EGKS L LE V VK av KPTVLI G L SG v GGAF T E E V V RA MA KS ner P I I F AL S N ------- P TS K a E CTAE day 154
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 305 ------ A IICT G ---------- RSDY P N Q V NN VLC FP F I FR GA LDV GA TA I NE EM K LAA VR A I A E L AHA E qsevvasayg 368
Cdd:cd05312 155 kwtdgr A LFAS G spfppveyng KTYV P G Q G NN AYI FP G I GL GA ILS GA RH I TD EM F LAA AE A L A S L VTD E ---------- 224
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16130388 369 dq D L SF G PE Y ii P KPFDP R L I - VK IA P AVAK A A M E S G V ATR P 409
Cdd:cd05312 225 -- E L AR G RL Y -- P PLSNI R E I s AQ IA V AVAK Y A Y E E G L ATR Y 262
NAD_bind_malic_enz
cd00762 NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
163-400
6.09e-28
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133442
Cd Length: 254
Bit Score: 113.47
E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 163 QH GTA IIST A AI L NG L R V VE K N IS DVRMVVS GAGAAA IACM NL L V A L ---- G LQ K H ---- N I VVC D S KG VIYQG R e PNMA 234
Cdd:cd00762 1 IQ GTA SVAV A GL L AA L K V TK K K IS EHKVLFN GAGAAA LGIA NL I V * L *vke G IS K E eack R I W*V D R KG LLVKN R - KETC 79
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 235 ETKAAY A VVDDGK R --- T L D D VI E -- GA D IFL G C S GP - KVL T Q E MVKKM A --- RA P M I L AL A NP EP -- E ILPPL A KEVRP 303
Cdd:cd00762 80 PNEYHL A RFANPE R esg D L E D AV E aa KP D FLI G V S RV g GAF T P E VIRA* A ein ER P V I F AL S NP TS ka E CTAEE A YTATE 159
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 304 - D AI ICT G RSD ---------- Y P N Q V NN VLC FP FIFR G ALDVGATA I NEEMK L A A VR AIA ELAHA E qsevvasaygdqdl 372
Cdd:cd00762 160 g R AI FAS G SPF hpvelnggty K P G Q G NN LYI FP GVAL G VILCRIRH I TDDVF L S A AE AIA SSVTE E -------------- 225
250 260
....*....|....*....|....*....
gi 16130388 373 S FG P EYII P KP FD PRLI - VK IA P AVAK A A 400
Cdd:cd00762 226 S LK P GRLY P PL FD IQEV s LN IA V AVAK Y A 254
Malic_M
pfam03949 Malic enzyme, NAD binding domain;
165-400
1.24e-23
Malic enzyme, NAD binding domain;
Pssm-ID: 427608 [Multi-domain]
Cd Length: 257
Bit Score: 100.73
E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 165 GTA IIST A AI L NG L RVVE K NI S DV R M V VS GAG A A A I ACMNLLVAL ---- GL QKH ---- N I VVC D SK G VIYQG RE ------ 230
Cdd:pfam03949 3 GTA AVAL A GL L AA L KITG K PL S EQ R I V FF GAG S A G I GIADQIRDA mvre GL SEE eark R I WMV D RQ G LLTDD RE dltdfq 82
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 231 ---- PNM AE T K AA yavvd DGKR TL DD V IEGA -- DIFL G C SG - P KVL T Q E M V KK MA RA --- P M I LA L A NP EP eilpp L A k E 300
Cdd:pfam03949 83 kpfa RKR AE L K GW ----- GDGI TL LE V VRKV kp TVLI G A SG v P GAF T E E I V RA MA AH ter P I I FP L S NP TS ----- K A - E 151
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 301 VR P D --------- A IIC TG ---------- RSDYPN Q V NN VLC FP FIFR GA LDVG A TA I NE EM K LAA VR A I A ELAHA E qse 361
Cdd:pfam03949 152 AT P E daykwtdgr A LFA TG spfppveyng KTYHIG Q G NN AYI FP GLGL GA IVSR A RR I TD EM F LAA AE A L A SYVDE E --- 228
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16130388 362 vvasaygdq DLSF G P ey II P KPF D P R LI - V KIA P AVAK A A 400
Cdd:pfam03949 229 --------- EPGQ G R -- LL P PLS D I R EV s R KIA V AVAK Y A 257
PRK05805
PRK05805 phosphate butyryltransferase; Validated
434-754
1.34e-11
phosphate butyryltransferase; Validated
Pssm-ID: 180267
Cd Length: 301
Bit Score: 66.27
E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 434 I F S Q A R - KA PK RVVLPEGEEAR VL H A TQ E LVT LG L A KP IL I G RPNV I EMRIQKLGLQIK agv DFEI VN n E S D P R fkeywt 512
Cdd:PRK05805 8 I L S K A K e QP PK TISVAVAQDEP VL E A VK E AKE LG I A NA IL V G DKEK I KEIAKEIDMDLE --- DFEI ID - E K D N R ------ 77
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 513 eyfqimkrrgvtq EQ A QR A lisnptvig AIM V QR G E AD AMIC G T V GDYHEHFS V VKNVF G Y R D G ------- V HTAGAMNA 585
Cdd:PRK05805 78 ------------- KA A LK A --------- VEL V SS G K AD MVMK G L V DTANFLRA V LNKEI G L R T G ktmshva V FEVPKYDR 135
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 586 LL lpsgnt F IA D TYV N DE PD AE E LAE I TLM A AETVRRF GIE - P R VA LLSHSNFGSSDC P SSSKM r QA L ELVRE R A -- PEL 662
Cdd:PRK05805 136 LL ------ F LT D AAF N IA PD LK E KID I INN A VTVAHAI GIE n P K VA PICAVEVVNPKM P ATLDA - AL L SKMSD R G qi KGC 208
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 663 MI DG EMHG D A AL V E AIRNDRMP D SSLK G S A N IL VM PN M EA ARIS Y NL L RVSSSE gv TV G PV L M G VAK PV h VLT PI A - S VR 741
Cdd:PRK05805 209 IV DG PLAL D N AL S E EAAKHKGI D GPVA G N A D IL LV PN I EA GNVM Y KT L TYFADC -- KN G GL L V G TSA PV - VLT SR A d S HE 285
330
....*....|...
gi 16130388 742 RIV N MV ALA VVE A 754
Cdd:PRK05805 286 TKL N SI ALA ALV A 298
PRK11890
PRK11890 phosphate acetyltransferase; Provisional
441-755
4.10e-05
phosphate acetyltransferase; Provisional
Pssm-ID: 183361
Cd Length: 312
Bit Score: 46.14
E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 441 A P KR V VL P EG E EA rv L HATQ E LVT LGL AK PIL I G RPNV IE MRIQKL GL QIK agv DF EIV NNES dprfkeywteyfqimkr 520
Cdd:PRK11890 23 L P TA V AH P CD E SS -- L RGAV E AAQ LGL IT PIL V G PRAR IE AVAAEC GL DLS --- GY EIV DAPH ----------------- 80
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 521 rgv TQEQ A QR A LI snptvigai M V QR GEA D A MIC G TVGDYHEHFS VV KNVF G Y R DG -------- VHTA G AMNA L llpsgn 592
Cdd:PRK11890 81 --- SHAA A AK A VE --------- L V RE GEA E A LMK G SLHTDELMSA VV ARDT G L R TE rrishvfv MDVP G YPKP L ------ 142
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 593 t F I A D TY VN DE P DA E EL A E I TLM A AETVRRF G I - EPRVA L LS HSNFGSSDC PS S ------ S KM RQ alelv R ERAPELMI D 665
Cdd:PRK11890 143 - I I T D AA VN IA P TL E DK A D I VQN A IDLAHAL G F d EPRVA I LS AVETVNPKI PS T ldaaal C KM AD ----- R GQITGAIL D 216
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130388 666 G EMHG D A A L - V EA I R NDRM p D S SLK G S A N ILV M P NM EA A risy N L L RVSSS -- E G VTVGPVLM G VAK P V h V LT PI A - SVR 741
Cdd:PRK11890 217 G PLAF D N A I s P EA A R IKGI - V S PVA G D A D ILV V P DL EA G ---- N M L AKQLT fl A G ADAAGIVL G ARV P I - I LT SR A d SVR 290
330
....*....|....
gi 16130388 742 RIVNMV A L A VVE A Q 755
Cdd:PRK11890 291 TRLASC A V A ALV A H 304
Blast search parameters
Data Source:
Precalculated data, version = cdd.v.3.21
Preset Options: Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
