ID A0A2C6CM77_9BACT Unreviewed; 399 AA.
AC A0A2C6CM77;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=CEQ90_14370 {ECO:0000313|EMBL:PHI19098.1};
OS Lewinellaceae bacterium SD302.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae.
OX NCBI_TaxID=2014804 {ECO:0000313|EMBL:PHI19098.1, ECO:0000313|Proteomes:UP000223945};
RN [1] {ECO:0000313|EMBL:PHI19098.1, ECO:0000313|Proteomes:UP000223945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD302 {ECO:0000313|EMBL:PHI19098.1,
RC ECO:0000313|Proteomes:UP000223945};
RA Wang K.;
RT "The draft genome sequence of Lewinellaceae bacterium SD302.";
RL Submitted (JUL-2017) 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}.
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:PHI19098.1}.
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DR EMBL; PDLQ01000023; PHI19098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6CM77; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000223945; 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; SFLDF00562; HemN-like__clustered_with_heat; 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:UP000223945};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..247
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 399 AA; 44824 MW; 92A82169E276FFE1 CRC64;
MLYLHIPFCK QACSYCNFHF STSSRGRDEL LLALHQEIRL RKEEIQRAGT ETIYLGGGTP
SLLTERELAD IFRVLAEVSD FDYQSSKVGK EHSKNANGPT DKREITLEAN PDDLTEATVE
ILAASPVNRL SIGLQSFQEK DLRYMNRAHS AKESTLAMQR VLKAGFTDLS VDLIYGSPTT
SDADWDDNIS RVLDFGVGHV SAYALTVEEK TALAHRIKTG QLPAPDEDRF ARQFDRLVER
LTLAGFEHYE ISNFAKPGQY SRHNTGYWQG KPYVGLGPSA HGFNGFDQRN WNIANNALYT
RLLTGATSIP AGLTETEQLS PTDRYNEFVM TGLRTQWGVR RTDLASKFGT SLAEYFSTTV
REEQLLCYFD SQKIESEGRY QLNQSGKRLA DGIAAALFR
//
