ID A0A0B7HG46_9FLAO Unreviewed; 350 AA.
AC A0A0B7HG46;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=CCYN2B_320044 {ECO:0000313|EMBL:CEN36553.1};
OS Capnocytophaga cynodegmi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=28189 {ECO:0000313|EMBL:CEN36553.1, ECO:0000313|Proteomes:UP000038055};
RN [1] {ECO:0000313|Proteomes:UP000038055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ccyn2B {ECO:0000313|Proteomes:UP000038055};
RA MANFREDI Pablo;
RL Submitted (JAN-2015) 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; CDOD01000026; CEN36553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7HG46; -.
DR STRING; 28189.CCYN74_200035; -.
DR eggNOG; COG0635; Bacteria.
DR Proteomes; UP000038055; 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 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 Oxidoreductase {ECO:0000313|EMBL:CEN36553.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000038055};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..205
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 350 AA; 39637 MW; 529E6458C6E59DCE CRC64;
MVSSICKELI LRKEEASNSQ LQTIYFGGGT PSILSFEELK TILQTIYENY NISPNAEVTL
EANPDDFFRD SSSPTQLLSN LKQLGINRLS IGVQSFYEED LRLMNRAHNA TQAELLLLEA
PKFFDNITID LIYGIPNMTD ERWQSNVRKA LSFGVPHISA YALTVEPKTA LHKFIALGKV
PNVNEQQAHS HFVSMISILE KEGFIHYEFS NFGKEGYFSR NNTAYWFGKK YMGIGPSAHS
FNGTERSWNI ANNIKYIEQI QKGIIPAEKE ILSQNDRYNE LIITRIRTMI GISVEEVETT
FGKKHADYLL LQAKKHITNG LLTINNKHLV TTTKGKFLSD GIAADLFIVD
//
