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MBHS_CITFR
ID   MBHS_CITFR              Reviewed;         375 AA.
AC   Q46045;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Hydrogenase-1 small chain;
DE            Short=HYD1;
DE            EC=1.12.99.6;
DE   AltName: Full=Membrane-bound hydrogenase 1 small subunit;
DE   AltName: Full=NiFe hydrogenase;
DE   Flags: Precursor;
GN   Name=hyaA;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yano K., Ikebukuro K., Tomiyama M., Karube I.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
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=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Periplasmic side.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; D28594; BAA05929.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46045; -.
DR   SMR; Q46045; -.
DR   STRING; 1333848.CFNIH1_11600; -.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.700; -; 1.
DR   Gene3D; 4.10.480.10; -; 1.
DR   InterPro; IPR027394; Cytochrome-c3_hydrogenase_C.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR037148; NiFe-Hase_small_C_sf.
DR   InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR   InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   PANTHER; PTHR30013; PTHR30013; 1.
DR   Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR   TIGRFAMs; TIGR00391; hydA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   3Fe-4S; 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Oxidoreductase; Signal.
FT   SIGNAL          1..47
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           48..375
FT                   /note="Hydrogenase-1 small chain"
FT                   /id="PRO_0000013426"
FT   REGION          353..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  40923 MW;  0B344C52BEF06E5C CRC64;
     MNTNNEETFY QAMRRKGVSR RSFLKYCSLA ATSLGLGAAM TPRIAWALEN KPRIPVVWIH
     GLECTCCTES FIRSSHPLAK DVILSLISLD YDDTLMAAAG TQAEEVFEDI LSRYHGRYIL
     AVEGNPPLGE QGMFCISGGR PFIEKAKRAA AGASAIIAWG TCASWGCVQA ARPNPTQATP
     IDKVITDKPI VKVPGCPPIP DVMSAIITYM VTFDRLPELD RLGRPLMFYG QRIHDKCYRR
     AHFDAGEFVE SWDDDAARKG YCLYKMGCKG PTTYNACSTT RWNGGVSFPI QSGHGCLGCS
     ENGFWDRGSF YSRVVDIPQM GTHSTADTVG LTALGVVASS VGVHAVASAV NQHNRHKQQL
     ADAGQQSPDN EDKQA
 
 
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