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Database: UniProt
Entry: A0A126T481_9GAMM
LinkDB: A0A126T481_9GAMM
Original site: A0A126T481_9GAMM 
ID   A0A126T481_9GAMM        Unreviewed;       376 AA.
AC   A0A126T481;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   ORFNames=JT25_008635 {ECO:0000313|EMBL:AMK76554.1};
OS   Methylomonas denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK76554.1, ECO:0000313|Proteomes:UP000030512};
RN   [1] {ECO:0000313|EMBL:AMK76554.1, ECO:0000313|Proteomes:UP000030512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJG1 {ECO:0000313|EMBL:AMK76554.1,
RC   ECO:0000313|Proteomes:UP000030512};
RX   PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA   Kits K.D., Klotz M.G., Stein L.Y.;
RT   "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT   Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT   FJG1.";
RL   Environ. Microbiol. 17:3219-3232(2015).
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; CP014476; AMK76554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A126T481; -.
DR   STRING; 1538553.JT25_008635; -.
DR   KEGG; mdn:JT25_008635; -.
DR   Proteomes; UP000030512; Chromosome.
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; HEME CHAPERONE-RELATED; 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:UP000030512};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..232
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   376 AA;  42161 MW;  944D7CC62CA6CDC4 CRC64;
     MLPLSLYIHF PWCIQKCPYC DFNSHAVKNP IPEEAYIDAV LTDLQADLEL LDAPRIIGSI
     FMGGGTPSLF SPEALRRLLT GIRQSVPVDE QCEFTLEANP GTFESAKFHE FRALGINRLS
     IGIQSFQDRH LRTLGRVHSA AEAKVAVEIA VKAGFDNFNL DLMFGLPDQS ESEALNDVET
     AISLAPTHIS FYQLTLEPNT YFYKFPPKLP EDDLIFAAQK RCQQLLADNG YQQYEVSAYA
     KPGKQSRHNR NYWQFGDYLG IGAGAHGKIS RALPNDILRT VKPRSPEQYL SQPGRSQCEA
     IDVAQLPLEF LMNQLRLKAG FSLSDYEVVT GLAADSLEPN LSVCLEQGLL RRQDSVYTCT
     EKGWDFLDVV LEKFVD
//
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