ID A0A372K5M0_9BURK Unreviewed; 405 AA.
AC A0A372K5M0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=D0B32_17705 {ECO:0000313|EMBL:RFU46878.1};
OS Paraburkholderia sp. DHOC27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2303330 {ECO:0000313|EMBL:RFU46878.1, ECO:0000313|Proteomes:UP000263097};
RN [1] {ECO:0000313|EMBL:RFU46878.1, ECO:0000313|Proteomes:UP000263097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOC27 {ECO:0000313|EMBL:RFU46878.1,
RC ECO:0000313|Proteomes:UP000263097};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOC27, isolated from subtropical forest soil.";
RL Submitted (AUG-2018) 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:RFU46878.1}.
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DR EMBL; QVQV01000004; RFU46878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372K5M0; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000263097; 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 SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 1.
DR SFLD; SFLDS00029; 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:UP000263097};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 23..256
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 405 AA; 45006 MW; 804F3FB343321C6B CRC64;
MKPAGKTGAG VIQAFTAPGS IHLTSLPPLA LYVHFPWCVR KCPYCDFNSH EWKGDAFPEN
DYLGALRTDL ELALPLVWGR QVHTVFIGGG TPSLLSAAGL DRLLSDVRAL LPLDADAEIT
LEANPGTFEA DKFAQFRASG VNRLSVGIQS FNEAHLKALG RIHDSAQARH AVDVAATTFD
NFNLDLMFAL PQQTLAECQA DIETALSFAP PHLSLYHLTL EPNTLFAKFP PALPDDDASA
DMQDWIHERT TAAGYERYEV SAYAQPQRQS KHNLNYWRFG DYLGIGAGAH TKLSFPNRIL
RQMRYKHPTT FIEQARAGAP VHEEHEVGTR DLPFEFMLNA LRLVEGFPVH RFIERTGMSM
TSIEPALQEA ERRGLIARTH EKIAPTPLGQ AFLNDLQALF LKEPQ
//
