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Database: UniProt
Entry: A0A3B0MNX5_9RHOB
LinkDB: A0A3B0MNX5_9RHOB
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ID   A0A3B0MNX5_9RHOB        Unreviewed;       384 AA.
AC   A0A3B0MNX5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   Name=hemN_1 {ECO:0000313|EMBL:SUZ31309.1};
GN   ORFNames=ROE7235_01047 {ECO:0000313|EMBL:SUZ31309.1};
OS   Roseibaca ekhonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Roseibaca.
OX   NCBI_TaxID=254356 {ECO:0000313|EMBL:SUZ31309.1, ECO:0000313|Proteomes:UP000272908};
RN   [1] {ECO:0000313|Proteomes:UP000272908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7235 {ECO:0000313|Proteomes:UP000272908};
RA   Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL   Submitted (AUG-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   -!- 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}.
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DR   EMBL; UIHC01000007; SUZ31309.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0MNX5; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000272908; 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; 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   Oxidoreductase {ECO:0000313|EMBL:SUZ31309.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272908};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          3..239
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   384 AA;  42064 MW;  58CC38EC5F61ED9E CRC64;
     MDDWQNGGFG LYVHWPFCQA KCPYCDFNSH FSAHVDQTAW ARAYLSEIDR IAAQTGPRVL
     NTIFFGGGTP SLMNPESVAA IIDRARACWP VANDLEITLE ANPTSVEAGR FRAFAAGGVN
     RISMGIQALN DDDLTRLGRL HSVAEARAAF DIARKTFDRV SFDLIYARQF QTLAAWQKEL
     SEALSMAVDH LSLYQLTIEP GTAFGARAAK GGLKGLPDDE IAADMYLATQ EICDRHGLPA
     YEVSNHARPG AQSRHNLIYW RYGDYAGIGP GAHGRLTLGG QRWATQTPLM PAIWLDQVGT
     LGHGEAPREA IPPEEQALEH IMMGLRLSEG LDIDRFAHLN GAPLPQSRID TLVEHGLLRQ
     AGARLTATPQ GRAVLNGILR ELLT
//
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