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 08-NOV-2023, entry version 104.
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; Pseudomonadota; 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P21853};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P21853};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:P21853};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P21853};
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; 4.10.480.10; Cytochrome-c3 hydrogenase, C-terminal domain; 1.
DR Gene3D; 3.40.50.700; NADH:ubiquinone oxidoreductase-like, 20kDa subunit; 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 NCBIfam; TIGR00391; hydA; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR30013:SF6; HYDROGENASE-1 SMALL CHAIN; 1.
DR PANTHER; PTHR30013; NIFE / NIFESE HYDROGENASE SMALL SUBUNIT FAMILY MEMBER; 1.
DR Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR PRINTS; PR00614; NIHGNASESMLL.
DR SUPFAM; SSF56770; HydA/Nqo6-like; 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|UniProtKB:P21853"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 234
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 237
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 262
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 277
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 296
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 299
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P21853"
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
//
