ID W7PWE9_9GAMM Unreviewed; 401 AA.
AC W7PWE9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN ORFNames=Q427_16665 {ECO:0000313|EMBL:EWH00950.1};
OS Halomonas sp. BC04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH00950.1, ECO:0000313|Proteomes:UP000019279};
RN [1] {ECO:0000313|EMBL:EWH00950.1, ECO:0000313|Proteomes:UP000019279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC04 {ECO:0000313|EMBL:EWH00950.1,
RC ECO:0000313|Proteomes:UP000019279};
RA Farooqui S., Greene A.C., Patel B.K.;
RT "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading
RT moderate Halophilic Bacterium.";
RL Submitted (DEC-2013) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:EWH00950.1}.
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DR EMBL; AZQX01000191; EWH00950.1; -; Genomic_DNA.
DR RefSeq; WP_043514717.1; NZ_AZQX01000191.1.
DR AlphaFoldDB; W7PWE9; -.
DR PATRIC; fig|1403540.3.peg.3115; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000019279; 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; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; 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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364116};
KW Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364116};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364116};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364116};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000019279};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 8..246
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 401 AA; 44229 MW; F3B033EA10CEAE60 CRC64;
MDTHPRQLDG LPPLALYVHV PWCVRKCPYC DFNSHGVGHG ADLPETRYLA ALLQDLEDDL
PLVGGRELTS IFIGGGTPSL MSAGFYERLF DVMATRLSLA SDIEITLEAN PGTLEQGRFQ
GYRSAGINRL SLGVQSFQDA QLRALGRIHS GGDAISAMDE ARHAGFDNVN LDLMHGLPGQ
TPALALADLD HALSLSPEHL SWYQLTLEPN TEFHSRPPVL PEEEVLWDIQ DRGHERLEAA
GLVRYEISAY ARPGLRSRHN LNYWRFGDYL GIGAGAHGKL SVADAQGRLH IERRWKARQP
EAYLRRCQDP RGFVAGRAGV EEDELPLEFA MNALRLVEGV SMRDWEAHTG RPAGALEARL
QSARKKGLLV EDGQRVQASP QGLLFLNELL VLIGEADAGT E
//
