FABV_YERPE
ID FABV_YERPE Reviewed; 399 AA.
AC Q8Z9U1; Q0W9T3; Q74PB4; Q7CFN5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000303|PubMed:22244758};
DE Short=ENR {ECO:0000303|PubMed:22244758};
DE EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
GN Name=fabV {ECO:0000303|PubMed:22244758};
GN OrderedLocusNames=YPO4104, y4119, YP_4011;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP NAD, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=22244758; DOI=10.1016/j.str.2011.07.019;
RA Hirschbeck M.W., Kuper J., Lu H., Liu N., Neckles C., Shah S., Wagner S.,
RA Sotriffer C.A., Tonge P.J., Kisker C.;
RT "Structure of the Yersinia pestis FabV enoyl-ACP reductase and its
RT interaction with two 2-pyridone inhibitors.";
RL Structure 20:89-100(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NAD.
RA Neckles C., Hirschbeck M.W., Shah S., Pan P., Bommineni G.R., Yu W.,
RA Liu N., Davoodi S., Kisker C., Tonge P.J.;
RT "Enoyl-ACP reductase from Yersinia pestis (wildtype) with cofactor NADH.";
RL Submitted (APR-2013) to the PDB data bank.
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-
CC carbon double bond in an enoyl moiety that is covalently linked to an
CC acyl carrier protein (ACP). {ECO:0000269|PubMed:22244758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01838};
CC -!- ACTIVITY REGULATION: Inhibited by 2-pyridone derivatives such as PT172
CC and PT173. {ECO:0000269|PubMed:22244758}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22244758}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; AL590842; CAL22672.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87661.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS64150.1; -; Genomic_DNA.
DR PIR; AD0498; AD0498.
DR RefSeq; WP_002215588.1; NZ_WUCM01000028.1.
DR RefSeq; YP_002348955.1; NC_003143.1.
DR PDB; 3ZU2; X-ray; 2.10 A; A=1-399.
DR PDB; 3ZU3; X-ray; 1.80 A; A=1-399.
DR PDB; 3ZU4; X-ray; 2.01 A; A=1-399.
DR PDB; 3ZU5; X-ray; 2.00 A; A=1-399.
DR PDB; 4BKQ; X-ray; 2.30 A; A=1-399.
DR PDB; 5G2O; X-ray; 1.90 A; A=1-399.
DR PDB; 5JAI; X-ray; 1.90 A; A=1-399.
DR PDB; 5JAM; X-ray; 2.00 A; A=1-399.
DR PDB; 5JAQ; X-ray; 1.90 A; A=1-399.
DR PDBsum; 3ZU2; -.
DR PDBsum; 3ZU3; -.
DR PDBsum; 3ZU4; -.
DR PDBsum; 3ZU5; -.
DR PDBsum; 4BKQ; -.
DR PDBsum; 5G2O; -.
DR PDBsum; 5JAI; -.
DR PDBsum; 5JAM; -.
DR PDBsum; 5JAQ; -.
DR AlphaFoldDB; Q8Z9U1; -.
DR SMR; Q8Z9U1; -.
DR IntAct; Q8Z9U1; 2.
DR STRING; 214092.YPO4104; -.
DR BindingDB; Q8Z9U1; -.
DR PaxDb; Q8Z9U1; -.
DR DNASU; 1149066; -.
DR EnsemblBacteria; AAM87661; AAM87661; y4119.
DR EnsemblBacteria; AAS64150; AAS64150; YP_4011.
DR GeneID; 66843634; -.
DR KEGG; ype:YPO4104; -.
DR KEGG; ypk:y4119; -.
DR KEGG; ypm:YP_4011; -.
DR PATRIC; fig|214092.21.peg.4646; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OMA; EGCIEQI; -.
DR BRENDA; 1.3.1.9; 4559.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR HAMAP; MF_01838; FabV_reductase; 1.
DR InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR PANTHER; PTHR37480; PTHR37480; 1.
DR Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR Pfam; PF12241; Enoyl_reductase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..399
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_0000220063"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838,
FT ECO:0000305|PubMed:22244758"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22244758, ECO:0000269|Ref.5"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT CONFLICT 233
FT /note="D -> Y (in Ref. 3; AAS64150)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3ZU2"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3ZU3"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3ZU3"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3ZU3"
FT TURN 232..237
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 239..259
FT /evidence="ECO:0007829|PDB:3ZU3"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 285..299
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5G2O"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:3ZU3"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:3ZU3"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:3ZU3"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3ZU3"
SQ SEQUENCE 399 AA; 43346 MW; 860F449EF0C24895 CRC64;
MIIKPRVRGF ICVTAHPTGC EANVKKQIDY VTTEGPIANG PKRVLVIGAS TGYGLAARIT
AAFGCGADTL GVFFERPGEE GKPGTSGWYN SAAFHKFAAQ KGLYAKSING DAFSDEIKQL
TIDAIKQDLG QVDQVIYSLA SPRRTHPKTG EVFNSALKPI GNAVNLRGLD TDKEVIKESV
LQPATQSEID STVAVMGGED WQMWIDALLD AGVLAEGAQT TAFTYLGEKI THDIYWNGSI
GAAKKDLDQK VLAIRESLAA HGGGDARVSV LKAVVTQASS AIPMMPLYLS LLFKVMKEKG
THEGCIEQVY SLYKDSLCGD SPHMDQEGRL RADYKELDPE VQNQVQQLWD QVTNDNIYQL
TDFVGYKSEF LNLFGFGIDG VDYDADVNPD VKIPNLIQG
