ID F5T228_9GAMM Unreviewed; 384 AA.
AC F5T228;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN ORFNames=MAMP_01276 {ECO:0000313|EMBL:EGL53553.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL53553.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL53553.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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:EGL53553.1}.
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DR EMBL; AFIG01000003; EGL53553.1; -; Genomic_DNA.
DR RefSeq; WP_007146803.1; NZ_AFIG01000003.1.
DR AlphaFoldDB; F5T228; -.
DR STRING; 1026882.MAMP_01276; -.
DR eggNOG; COG0635; Bacteria.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000003544; 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; 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 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|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:UP000003544};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 4..236
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 384 AA; 43419 MW; 40FDD4AC78681A11 CRC64;
MFNFTSLPPL SLYIHVPWCV RKCPYCDFNS HDNHQSLPEQ AYIDALIRDL EQELPLIWGR
SINTVFIGGG TPSLFSAEAY DRLFSSVRAL LPLQHDAEIT LEANPGTVEA GRFSEYRDVG
INRLSIGIQS FDQDALQSLG RIHDSKQAIK AVEYAHQAGF DSFNLDLMFG LPGQDEKKAR
HDVETAIALA PPHISYYQLT IEPNTLFYAQ PPSLPDDDPI YDWQLANQAR LAEAGYMQYE
TSAYAQKGHQ CRHNINYWRY GDYIGIGAGA HGKISSASPQ QIQRRVKQKQ PQKYIDTAGT
EAGLLEQTFV SEDEVGFEFM LNAMRLLDGV PTPLFQQHTG LPISTIKQAM QKAEQLELLQ
HTIERIRPTE KGQRYLNSLI ELFI
//
