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Database: UniProt
Entry: A0A3M8SYW0_9GAMM
LinkDB: A0A3M8SYW0_9GAMM
Original site: A0A3M8SYW0_9GAMM 
ID   A0A3M8SYW0_9GAMM        Unreviewed;       384 AA.
AC   A0A3M8SYW0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   Name=hemW {ECO:0000313|EMBL:RNF85885.1};
GN   ORFNames=EER27_00070 {ECO:0000313|EMBL:RNF85885.1};
OS   Lysobacter psychrotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1327343 {ECO:0000313|EMBL:RNF85885.1, ECO:0000313|Proteomes:UP000267049};
RN   [1] {ECO:0000313|EMBL:RNF85885.1, ECO:0000313|Proteomes:UP000267049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS60 {ECO:0000313|EMBL:RNF85885.1,
RC   ECO:0000313|Proteomes:UP000267049};
RA   Luo Y., Sheng H.;
RT   "Lysobacter cryohumiis sp. nov., isolated from soil in the Tianshan
RT   Mountains, Xinjiang, China.";
RL   Submitted (NOV-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   -!- 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:RNF85885.1}.
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DR   EMBL; RIBS01000001; RNF85885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8SYW0; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000267049; 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; SFLDG01082; B12-binding_domain_containing; 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:UP000267049};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..234
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   384 AA;  42207 MW;  9E9458A259F3497F CRC64;
     MLTTPPLSLY VHVPWCVRKC PYCDFNSHEG RGELPFAAYV DALLADLDHD LPLVWGRVVH
     SVFFGGGTPS LMPPEFIDRF LQGASSRLRM APGCEITLET NPGTAEHGRF GGYRAAGVNR
     LSFGIQSFDD GCLKRLGRIH DAAQADAAVK LAQDAGFDNF NLDLMYALPG QTLAMAERDL
     ERAFALQPTH VSHYQLTLEP NTVFAARPPA GIPAEDDSWD MQEHCQAMLA AAGYGQYEVS
     AYAQPERQCA HNLNYWKYGD YLGIGAGAHA KITLGSEQDI LRRWKLKHPT AYLAHAGTDA
     AIGGDERITL QRRPFEFMLN ALRLVDGFSL TRFEASTGLP RAQIGAQLAQ AEANGWLAIE
     ADLVRPTELG RRFTNDVVAL FLGD
//
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