ID A0A1I0G4Y9_9BACI Unreviewed; 383 AA.
AC A0A1I0G4Y9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=SAMN05421676_106191 {ECO:0000313|EMBL:SET65095.1};
OS Salinibacillus kushneri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX NCBI_TaxID=237682 {ECO:0000313|EMBL:SET65095.1, ECO:0000313|Proteomes:UP000199095};
RN [1] {ECO:0000313|EMBL:SET65095.1, ECO:0000313|Proteomes:UP000199095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SET65095.1,
RC ECO:0000313|Proteomes:UP000199095};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to an
CC unknown acceptor. Binds one molecule of heme per monomer, possibly
CC covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|RuleBase:RU364116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364116}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000256|ARBA:ARBA00006100}.
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DR EMBL; FOHJ01000006; SET65095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0G4Y9; -.
DR STRING; 237682.SAMN05421676_106191; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000199095; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR004559; HemW-like.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR NCBIfam; TIGR00539; hemN_rel; 1.
DR PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR PANTHER; PTHR13932:SF5; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU364116};
KW Chaperone {ECO:0000256|RuleBase:RU364116};
KW Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW Heme {ECO:0000256|RuleBase:RU364116}; Iron {ECO:0000256|RuleBase:RU364116};
KW Iron-sulfur {ECO:0000256|RuleBase:RU364116};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364116};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..232
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 383 AA; 44436 MW; 38CA3BBA492659E7 CRC64;
MVQSVYIHIP FCHEICHYCD FTKIYYNESL ANQYLDALQK EIKLYIGEQK RHVKTIYIGG
GTPTSLSDPQ FEKLLRIVNQ YFDVSSCNEF TVEANPGEFS QEKAKMLKDY GVNRISLGVQ
VLDDEFLKTL NRNHQVRDVD QTVQALQSNG LTNISMDFIY ALPNQTLEHF EKTLQAALDY
QLPHYSAYAL QIEPKTVFYI RYKKGKLSKP PEDVEADMYE SLVNKMENHG LYHYEISNFG
KPGYESQHNL VYWDNAYYFG FGAGAHGYIN GKRLVNLRPV NHYIDSLMKD EKPVLHEEMI
TKKEQIEEEM FLGLRKSQGV SKSAFYRKYG ITMKNLYHEE IDQLKQKGWL VEAQDAVKLT
PQGRLFGNEV FASFLLDKDV IIS
//
