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Database: UniProt
Entry: A0A0N7J8A4_9BURK
LinkDB: A0A0N7J8A4_9BURK
Original site: A0A0N7J8A4_9BURK 
ID   A0A0N7J8A4_9BURK        Unreviewed;       403 AA.
AC   A0A0N7J8A4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   Name=hemN_1 {ECO:0000313|EMBL:ALK87640.1};
GN   ORFNames=L63ED372_00412 {ECO:0000313|EMBL:ALK87640.1};
OS   Limnohabitans sp. 63ED37-2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK87640.1, ECO:0000313|Proteomes:UP000059510};
RN   [1] {ECO:0000313|EMBL:ALK87640.1, ECO:0000313|Proteomes:UP000059510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK87640.1,
RC   ECO:0000313|Proteomes:UP000059510};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) 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; CP011774; ALK87640.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N7J8A4; -.
DR   STRING; 1678128.L63ED372_00412; -.
DR   KEGG; lih:L63ED372_00412; -.
DR   PATRIC; fig|1678128.3.peg.411; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000059510; 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; 3.20.20.70; 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:ALK87640.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059510};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          18..254
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   403 AA;  44944 MW;  FD72F13F9C7F0B6A CRC64;
     MSDMMDPVHA MRPGVLQLNA LPPLSLYVHL PWCIKKCPYC DFNSHEFREG ADPVSTQDAY
     INALFADLEA SLPLIWGRSI QTVFLGGGTP SLFSPEAIDR LISGIRARVR LAPDAEITME
     ANPGTFEKDR FKAFHQAGIT RLSIGVQSFD NAHLKALGRV HDRDQALAAV TEAAQVFDTF
     NLDLMYALPG QKLEGLTQDI QTALGFAPPH ISIYHLTIEP NTVFAKFPPT LPEDDLAYEM
     MDRITELTAS AGLDRYEVSA YAKPGHQCAH NLNYWQFGDY LGIGAGAHSK LSFAHRVMRQ
     VRYREPALYM QQAIKGEPVT QSTEVSRQDL PFEFMLNALR LRGGFDLADY VDRTGLAMTS
     IQKGLQEAER LGLIGRDLHR VWPTEKGFDF LSDLQALFLS EAP
//
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