ID A1AP38_PELPD Unreviewed; 473 AA.
AC A1AP38;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Iron-only hydrogenase maturation protein HydG {ECO:0000313|EMBL:ABK99108.1};
GN OrderedLocusNames=Ppro_1492 {ECO:0000313|EMBL:ABK99108.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99108.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK99108.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000482; ABK99108.1; -; Genomic_DNA.
DR AlphaFoldDB; A1AP38; -.
DR STRING; 338966.Ppro_1492; -.
DR KEGG; ppd:Ppro_1492; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_0_0_7; -.
DR OrthoDB; 3320990at2; -.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR024007; FeFe-hyd_mat_HydG.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR03955; rSAM_HydG; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 1.
DR SMART; SM00876; BATS; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 81..325
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 473 AA; 52636 MW; 446EA18999534185 CRC64;
MSSLPSMKLS AGAADFIDEA YLFGLLGGKR PEAARVRDII AKSLEKQALG VEETAQLLLA
DTPELVEEIF AAARELKEKV YGNRIVLFAP LYIGNKCVND CAYCAFKRSN ASAIRRTLTE
GEIRGQVEAL ESKGHKRLIL VFGEHQAYDA EFIAQSVRTV YDTRGKGEIR RVNINAAPLD
REGYAIVKAA GIGTYQIFHE TYHHETYARL HPRGTRKANY LYRLDGLNRA FEAGCDDVGL
GVLFGLVDWR FEVLGLVSHA LHLQRRYNVG PHTISFPRLR PAAGVALDRE LLVGDQEFKR
IIAILRLAVP YTGLILTARE NAQVRRECIS LGVSQIDAGS RIELGGYTEA GDAQVMEREQ
FSLGDVRSLD EVMAELMGAG YIPSFCTSCY RVGRTGEHFM EFSIPGFIKE FCTPNALLTL
QEYLLDYASP STREIGDRLI AEELAKLVDG HGKQGVVQRL KEIREGAQRD HCF
//
