MBHM_ECOLI
ID MBHM_ECOLI Reviewed; 567 AA.
AC P0ACE0; P37181; Q2M9K1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hydrogenase-2 large chain;
DE Short=HYD2;
DE EC=1.12.99.6;
DE AltName: Full=Membrane-bound hydrogenase 2 large subunit;
DE AltName: Full=NiFe hydrogenase;
DE Flags: Precursor;
GN Name=hybC; OrderedLocusNames=b2994, JW2962;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / TG1;
RX PubMed=8021226; DOI=10.1128/jb.176.14.4416-4423.1994;
RA Menon N.K., Chatelus C.Y., Dervartanian M., Wendt J.C., Shanmugam K.T.,
RA Peck H.D. Jr., Przybyla A.E.;
RT "Cloning, sequencing, and mutational analysis of the hyb operon encoding
RT Escherichia coli hydrogenase 2.";
RL J. Bacteriol. 176:4416-4423(1994).
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 PROTEIN SEQUENCE OF 2-7.
RX PubMed=9738917; DOI=10.1046/j.1432-1327.1998.2550746.x;
RA Sargent F., Ballantine S.P., Rugman P.A., Palmer T., Boxer D.H.;
RT "Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small
RT subunit -- identification of a soluble precursor of the small subunit in a
RT hypB mutant.";
RL Eur. J. Biochem. 255:746-754(1998).
CC -!- FUNCTION: This is one of three E.coli hydrogenases synthesized in
CC response to different physiological conditions. HYD2 is involved in
CC hydrogen uptake.
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 P0ACE0; P0AAM7: hybG; NbExp=2; IntAct=EBI-549849, EBI-562426;
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; U09177; AAA21591.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69161.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76030.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77055.1; -; Genomic_DNA.
DR PIR; C55516; C55516.
DR RefSeq; NP_417468.1; NC_000913.3.
DR RefSeq; WP_000083065.1; NZ_STEB01000001.1.
DR PDB; 6EHQ; X-ray; 2.20 A; L/M=1-552.
DR PDB; 6EHS; X-ray; 1.50 A; L/M=1-552.
DR PDB; 6EN9; X-ray; 1.50 A; L/M=1-567.
DR PDB; 6G7M; X-ray; 1.71 A; L/M=1-567.
DR PDB; 6GAM; X-ray; 1.40 A; L/M=1-567.
DR PDB; 6GAN; X-ray; 1.60 A; L/M=1-567.
DR PDB; 6SYO; X-ray; 1.25 A; LLL/MMM=1-567.
DR PDB; 7NEM; X-ray; 1.35 A; L/M=1-567.
DR PDBsum; 6EHQ; -.
DR PDBsum; 6EHS; -.
DR PDBsum; 6EN9; -.
DR PDBsum; 6G7M; -.
DR PDBsum; 6GAM; -.
DR PDBsum; 6GAN; -.
DR PDBsum; 6SYO; -.
DR PDBsum; 7NEM; -.
DR AlphaFoldDB; P0ACE0; -.
DR SMR; P0ACE0; -.
DR BioGRID; 4262375; 28.
DR ComplexPortal; CPX-282; Hydrogenase-2 complex.
DR DIP; DIP-36022N; -.
DR IntAct; P0ACE0; 16.
DR STRING; 511145.b2994; -.
DR jPOST; P0ACE0; -.
DR PaxDb; P0ACE0; -.
DR PRIDE; P0ACE0; -.
DR EnsemblBacteria; AAC76030; AAC76030; b2994.
DR EnsemblBacteria; BAE77055; BAE77055; BAE77055.
DR GeneID; 66673108; -.
DR GeneID; 945182; -.
DR KEGG; ecj:JW2962; -.
DR KEGG; eco:b2994; -.
DR PATRIC; fig|1411691.4.peg.3735; -.
DR EchoBASE; EB1749; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_6; -.
DR InParanoid; P0ACE0; -.
DR OMA; AMFRGFE; -.
DR PhylomeDB; P0ACE0; -.
DR BioCyc; EcoCyc:HYBC-MON; -.
DR BioCyc; MetaCyc:HYBC-MON; -.
DR PRO; PR:P0ACE0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0044569; C:[Ni-Fe] hydrogenase complex; IC:ComplexPortal.
DR GO; GO:0031236; C:extrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
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; ISM:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProt.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9738917"
FT CHAIN 2..552
FT /note="Hydrogenase-2 large chain"
FT /id="PRO_0000013407"
FT PROPEP 553..567
FT /id="PRO_0000013408"
FT BINDING 61
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 64
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 546
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 549
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT SITE 552..553
FT /note="Cleavage; by HybD"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 86..109
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 181..209
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6EHQ"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6EHQ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6G7M"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:6EHQ"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 392..409
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 421..451
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 468..477
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 480..489
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 492..499
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 501..506
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 547..551
FT /evidence="ECO:0007829|PDB:6GAM"
SQ SEQUENCE 567 AA; 62491 MW; A19E6F513390F29E CRC64;
MSQRITIDPV TRIEGHLRID CEIENGVVSK AWASGTMWRG MEEIVKNRDP RDAWMIVQRI
CGVCTTTHAL SSVRAAESAL NIDVPVNAQY IRNIILAAHT THDHIVHFYQ LSALDWVDIT
SALQADPTKA SEMLKGVSTW HLNSPEEFTK VQNKIKDLVA SGQLGIFANG YWGHPAMKLP
PEVNLIAVAH YLQALECQRD ANRVVALLGG KTPHIQNLAV GGVANPINLD GLGVLNLERL
MYIKSFIDKL SDFVEQVYKV DTAVIAAFYP EWLTRGKGAV NYLSVPEFPT DSKNGSFLFP
GGYIENADLS SYRPITSHSD EYLIKGIQES AKHSWYKDEA PQAPWEGTTI PAYDGWSDDG
KYSWVKSPTF YGKTVEVGPL ANMLVKLAAG RESTQNKLNE IVAIYQKLTG NTLEVAQLHS
TLGRIIGRTV HCCELQDILQ NQYSALITNI GKGDHTTFVK PNIPATGEFK GVGFLEAPRG
MLSHWMVIKD GIISNYQAVV PSTWNSGPRN FNDDVGPYEQ SLVGTPVADP NKPLEVVRTI
HSFDPCMACA VHVVDADGNE VVSVKVL
