ID A0A438AH26_9RHOB Unreviewed; 401 AA.
AC A0A438AH26;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=EKE94_11195 {ECO:0000313|EMBL:RVV98023.1};
OS Mesobaculum littorinae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mesobaculum.
OX NCBI_TaxID=2486419 {ECO:0000313|EMBL:RVV98023.1, ECO:0000313|Proteomes:UP000285908};
RN [1] {ECO:0000313|EMBL:RVV98023.1, ECO:0000313|Proteomes:UP000285908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0103 {ECO:0000313|EMBL:RVV98023.1,
RC ECO:0000313|Proteomes:UP000285908};
RA Li F.;
RT "Mesobaculum littorinae gen. nov., sp. nov., isolated from Littorina scabra
RT that represents a novel genus of the order Rhodobacteraceae.";
RL Submitted (NOV-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:RVV98023.1}.
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DR EMBL; RQXX01000003; RVV98023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438AH26; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000285908; 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:UP000285908};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 20..256
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 401 AA; 43809 MW; E374228AEC624BC5 CRC64;
MSLAIVPLPS ENSSPPVSED WRNGGFGLYV HWPFCQAKCP YCDFNSHVVS GVDQTRWARA
LVSEIDRYAA LTPERRLSSI FFGGGTPSLM EPATVEAVIA AAQRQWNFSN DIEITLEANP
TSVEADRFVG YRAAGVNRVS MGIQSLDDTS LRALGRLHTA AEALAAFDVA RSTFDRVSFD
LIYARQHQSA REWEAELRRA LSFDLDHLSV YQLTIEPNTA FGDRFSRNRL PGLPDEDLGA
DMWVITQDLC LSAGLPAYEV SNHARPGSES RHNQIYWRYG DYVGVGPGAH GRVTTTARTA
TAAVTQPGKW LADVEAGVAP DTTELLSPQE QAEEYLLMGL RLSEGISLNR IGSLNPQALN
QTALSDLLAN GFLEECDGQL RTTAAGRPLL NAILARLAAS P
//
