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Database: UniProt
Entry: A0A0S9N3Q7_9BURK
LinkDB: A0A0S9N3Q7_9BURK
Original site: A0A0S9N3Q7_9BURK 
ID   A0A0S9N3Q7_9BURK        Unreviewed;       422 AA.
AC   A0A0S9N3Q7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   ORFNames=ASF44_09370 {ECO:0000313|EMBL:KQP39912.1};
OS   Pseudorhodoferax sp. Leaf274.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP39912.1, ECO:0000313|Proteomes:UP000051759};
RN   [1] {ECO:0000313|EMBL:KQP39912.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP39912.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP39912.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP39912.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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   -!- 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:KQP39912.1}.
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DR   EMBL; LMNA01000023; KQP39912.1; -; Genomic_DNA.
DR   RefSeq; WP_056900709.1; NZ_LMNA01000023.1.
DR   AlphaFoldDB; A0A0S9N3Q7; -.
DR   STRING; 1736318.ASF44_09370; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000051759; 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   Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          20..274
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   422 AA;  46514 MW;  2A57735B7C99AC7D CRC64;
     MSGLRPRELT AYTRPGLLQL QAQPPLALYL HLPWCIRKCP YCDFNSHAVR GDEAVVRWAG
     ADAPAVTQVA APAELPEQRY IDALIADLEA ALPLVWGRTV HSIFIGGGTP SLFSPQAIDR
     LLGDVRARLR LEADCEITLE ANPGTFEKDR FRAYRAAGVT RLSVGVQSFD DALLQAVGRV
     HDRRQAISAL EEARQAFDTF NLDLMYALPG QTPEMLAQDL ATALALAPPH LSVYHLTIEP
     NTFFAKHPPV LPEDDTAYAM LDQITEATGR AGLERYEVSA YARAGHRCVH NLNYWQFGDY
     LGIGAGAHSK LSFAHRVVRQ VRLREPGLYM AQALAGAALA QDDDVRRADL PFEFMLNALR
     LREGFALQDF TERTGLPLSS IAAGLAEGER RGLLLRDAAR VRPSEKGFDF LSDLQEIFLS
     GA
//
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