ID A0A0E9M166_9BACT Unreviewed; 342 AA.
AC A0A0E9M166;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=JCM15548_13657 {ECO:0000313|EMBL:GAO31308.1};
OS Geofilum rubicundum JCM 15548.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Geofilum.
OX NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO31308.1, ECO:0000313|Proteomes:UP000032900};
RN [1] {ECO:0000313|EMBL:GAO31308.1, ECO:0000313|Proteomes:UP000032900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO31308.1};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO31308.1}.
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DR EMBL; BAZW01000043; GAO31308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9M166; -.
DR STRING; 1236989.JCM15548_13657; -.
DR Proteomes; UP000032900; 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; 3.30.750.200; -; 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 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 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|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000032900};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..202
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 342 AA; 39435 MW; 765093F36A34A25A CRC64;
MEPFFNTLKQ EIVHYAPLFT NRIETLYFGG GTPSLLKSGM YTELFLLLKS YYSFNTDVEI
TIEANPDDLT PTYIDDLLAL GFNRISIGIQ SFNETDLQEM GRRHSSSQAL QSIQNAYNGG
FRNIGMDLIY GLPWSSTEAF EKNLEIFKTL PVNHLSAYHL TFEEGTPFER LLKRGVYQEM
KDNKSLAQYE LLCRLTANNG FEHYEVSNFS QPGYRSRHNS SYWNGSPYIG FGPGSHSYYK
GKRSWNKPDL ATYNKGHWAD ITEEETLNKD DLFNESIMLG LRTSDGIDLE QLQNLHPAFY
EAFSKKQIKW LTAGDLYLAK NRLICHEKSW FIVDSIIKDL FI
//
