MBHL_ECOLI
ID MBHL_ECOLI Reviewed; 597 AA.
AC P0ACD8; P19927; P78056;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Hydrogenase-1 large chain;
DE Short=HYD1;
DE EC=1.12.99.6;
DE AltName: Full=Membrane-bound hydrogenase 1 large subunit;
DE AltName: Full=NiFe hydrogenase;
GN Name=hyaB; OrderedLocusNames=b0973, JW0955;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX PubMed=2180913; DOI=10.1128/jb.172.4.1969-1977.1990;
RA Menon N.K., Robbins J., Peck H.D. Jr., Chatelus C.Y., Choi E.-S.,
RA Przybyla A.E.;
RT "Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1
RT operon containing six open reading frames.";
RL J. Bacteriol. 172:1969-1977(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-597.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
CC -!- FUNCTION: This is one of three E.coli hydrogenases synthesized in
CC response to different physiological conditions. HYD1 is believed to
CC have a role in hydrogen cycling during fermentative growth.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC -!- INTERACTION:
CC P0ACD8; P69739: hyaA; NbExp=6; IntAct=EBI-851493, EBI-9124108;
CC P0ACD8; P19930: hyaD; NbExp=3; IntAct=EBI-851493, EBI-552940;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
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DR EMBL; M34825; AAA23998.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74058.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35738.2; -; Genomic_DNA.
DR PIR; C64838; HQECL.
DR RefSeq; NP_415492.1; NC_000913.3.
DR RefSeq; WP_000107384.1; NZ_STEB01000006.1.
DR PDB; 3UQY; X-ray; 1.47 A; L/M=1-582.
DR PDB; 3USC; X-ray; 2.00 A; L/M=1-582.
DR PDB; 3USE; X-ray; 1.67 A; L/M=1-582.
DR PDB; 4GD3; X-ray; 3.30 A; J/K/L/M=1-582.
DR PDB; 4UE3; X-ray; 1.40 A; L/M=1-582.
DR PDB; 5A4F; X-ray; 1.25 A; L/M=1-582.
DR PDB; 5A4I; X-ray; 1.23 A; L/M=1-582.
DR PDB; 5A4M; X-ray; 1.70 A; L/M=1-582.
DR PDB; 5ADU; X-ray; 1.10 A; L/M=1-582.
DR PDB; 5JRD; X-ray; 1.20 A; L/M=1-582.
DR PDB; 5LMM; X-ray; 1.20 A; L/M=1-582.
DR PDB; 5LRY; X-ray; 1.40 A; L/M=1-582.
DR PDB; 6FPI; X-ray; 1.50 A; L/M=1-582.
DR PDB; 6FPO; X-ray; 1.05 A; L/M=1-582.
DR PDB; 6FPW; X-ray; 1.35 A; L/M=1-582.
DR PDB; 6G7R; X-ray; 1.20 A; L/M=1-582.
DR PDB; 6G94; X-ray; 2.50 A; J/K/L/M=1-582.
DR PDB; 6GAL; X-ray; 1.25 A; L/M=1-582.
DR PDB; 6RP2; X-ray; 1.35 A; L/M=1-582.
DR PDBsum; 3UQY; -.
DR PDBsum; 3USC; -.
DR PDBsum; 3USE; -.
DR PDBsum; 4GD3; -.
DR PDBsum; 4UE3; -.
DR PDBsum; 5A4F; -.
DR PDBsum; 5A4I; -.
DR PDBsum; 5A4M; -.
DR PDBsum; 5ADU; -.
DR PDBsum; 5JRD; -.
DR PDBsum; 5LMM; -.
DR PDBsum; 5LRY; -.
DR PDBsum; 6FPI; -.
DR PDBsum; 6FPO; -.
DR PDBsum; 6FPW; -.
DR PDBsum; 6G7R; -.
DR PDBsum; 6G94; -.
DR PDBsum; 6GAL; -.
DR PDBsum; 6RP2; -.
DR AlphaFoldDB; P0ACD8; -.
DR SMR; P0ACD8; -.
DR BioGRID; 4260043; 18.
DR BioGRID; 849954; 1.
DR ComplexPortal; CPX-281; Hydrogenase-1 complex.
DR DIP; DIP-36180N; -.
DR IntAct; P0ACD8; 10.
DR STRING; 511145.b0973; -.
DR jPOST; P0ACD8; -.
DR PaxDb; P0ACD8; -.
DR PRIDE; P0ACD8; -.
DR EnsemblBacteria; AAC74058; AAC74058; b0973.
DR EnsemblBacteria; BAA35738; BAA35738; BAA35738.
DR GeneID; 66670751; -.
DR GeneID; 945580; -.
DR KEGG; ecj:JW0955; -.
DR KEGG; eco:b0973; -.
DR PATRIC; fig|1411691.4.peg.1301; -.
DR EchoBASE; EB0464; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_6; -.
DR InParanoid; P0ACD8; -.
DR OMA; EEVTHSW; -.
DR PhylomeDB; P0ACD8; -.
DR BioCyc; EcoCyc:HYAB-MON; -.
DR BioCyc; MetaCyc:HYAB-MON; -.
DR BRENDA; 1.12.99.6; 2026.
DR PRO; PR:P0ACD8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0044569; C:[Ni-Fe] hydrogenase complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IDA:ComplexPortal.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0016151; F:nickel cation binding; IDA:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IDA:ComplexPortal.
DR GO; GO:0006113; P:fermentation; IDA:ComplexPortal.
DR Gene3D; 1.10.645.10; -; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane;
KW Metal-binding; Nickel; Oxidoreductase; Reference proteome.
FT CHAIN 1..597
FT /note="Hydrogenase-1 large chain"
FT /id="PRO_0000199712"
FT BINDING 76
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 79
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 576
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 579
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT CONFLICT 52
FT /note="M -> I (in Ref. 1; AAA23998)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="W -> R (in Ref. 1; AAA23998)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6FPO"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 101..125
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 196..216
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 254..273
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6FPO"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 412..421
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 425..437
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 448..478
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 497..507
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 510..519
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 522..529
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 547..552
FT /evidence="ECO:0007829|PDB:6FPO"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:4GD3"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:6FPO"
FT HELIX 577..581
FT /evidence="ECO:0007829|PDB:6FPO"
SQ SEQUENCE 597 AA; 66253 MW; 659DD7EDE16D6342 CRC64;
MSTQYETQGY TINNAGRRLV VDPITRIEGH MRCEVNINDQ NVITNAVSCG TMFRGLEIIL
QGRDPRDAWA FVERICGVCT GVHALASVYA IEDAIGIKVP DNANIIRNIM LATLWCHDHL
VHFYQLAGMD WIDVLDALKA DPRKTSELAQ SLSSWPKSSP GYFFDVQNRL KKFVEGGQLG
IFRNGYWGHP QYKLPPEANL MGFAHYLEAL DFQREIVKIH AVFGGKNPHP NWIVGGMPCA
INIDESGAVG AVNMERLNLV QSIITRTADF INNVMIPDAL AIGQFNKPWS EIGTGLSDKC
VLSYGAFPDI ANDFGEKSLL MPGGAVINGD FNNVLPVDLV DPQQVQEFVD HAWYRYPNDQ
VGRHPFDGIT DPWYNPGDVK GSDTNIQQLN EQERYSWIKA PRWRGNAMEV GPLARTLIAY
HKGDAATVES VDRMMSALNL PLSGIQSTLG RILCRAHEAQ WAAGKLQYFF DKLMTNLKNG
NLATASTEKW EPATWPTECR GVGFTEAPRG ALGHWAAIRD GKIDLYQCVV PTTWNASPRD
PKGQIGAYEA ALMNTKMAIP EQPLEILRTL HSFDPCLACS THVLGDDGSE LISVQVR
