ID A0A080M9T5_9PROT Unreviewed; 416 AA.
AC A0A080M9T5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN Name=hemN_1 {ECO:0000313|EMBL:KFB77741.1};
GN ORFNames=AW06_001116 {ECO:0000313|EMBL:KFB77741.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77741.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77741.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:KFB77741.1}.
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DR EMBL; JDST02000018; KFB77741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M9T5; -.
DR STRING; 1453999.AW06_001116; -.
DR Proteomes; UP000021315; 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; SFLDG01065; anaerobic_coproporphyrinogen-I; 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|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 Oxidoreductase {ECO:0000313|EMBL:KFB77741.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 28..267
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 416 AA; 45621 MW; EA861C9C0F2B0BEA CRC64;
MPGSRSRMII PLLPQARLAA IKEPEPRFRS PPPLSLYVHI PWCVQKCPYC DFNSHSLQVG
SSTAPTAIPE SDYLAALVAD LESALPLVWG RRIDSLFFGG GTPSLLSGAG LDQLLAALRS
RLTFLPGAEI TLEANPGTVE AARFAAFRDA GINRLSLGIQ SFNPQHLKAL GRIHDDHEAR
RAITIAARHF DNFNLDLMYG LPGQTLAEAL ADLDAALAFS PPHLSCYQLT IEANTAFAAR
PPALPEDDLC ADMQDAIEAR LAAAGYLHYE TSAFAIPGRQ CQHNLNYWHF GDYLGIGAGA
HGKLTLHDRV LRQMRWKGPE QYLAQVAAGM PVQEEFAVAA ADLPFEFMIN ALRLVQGFDA
QIFESRTALS LLSIEGKLRQ AEQEGLIERQ RQRIVPSEHG RRFLNRLLVG FLADAG
//
