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Database: UniProt
Entry: A0A2T4IBL9_9RHOO
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Original site: A0A2T4IBL9_9RHOO 
ID   A0A2T4IBL9_9RHOO        Unreviewed;       409 AA.
AC   A0A2T4IBL9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=C8261_15865 {ECO:0000313|EMBL:PTD95177.1};
OS   Pseudothauera lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Pseudothauera.
OX   NCBI_TaxID=2136175 {ECO:0000313|EMBL:PTD95177.1, ECO:0000313|Proteomes:UP000241193};
RN   [1] {ECO:0000313|EMBL:PTD95177.1, ECO:0000313|Proteomes:UP000241193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D20 {ECO:0000313|EMBL:PTD95177.1,
RC   ECO:0000313|Proteomes:UP000241193};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PTD95177.1, ECO:0000313|Proteomes:UP000241193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D20 {ECO:0000313|EMBL:PTD95177.1,
RC   ECO:0000313|Proteomes:UP000241193};
RA   Liang Q.-Y.;
RT   "Thauera lacus sp. nov., isolated from an saline lake in Inner Mongolia,
RT   China.";
RL   Submitted (APR-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}.
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:PTD95177.1}.
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DR   EMBL; PZKC01000017; PTD95177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4IBL9; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000241193; 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; 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|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   Reference proteome {ECO:0000313|Proteomes:UP000241193};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          28..261
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  43961 MW;  4EE72AB4E8661650 CRC64;
     MSTRRIIPLT PASPPAAPHP PPTATPHPPA PPPLAVYVHY PWCVRKCPYC DFNSHTARAA
     APPEAAYLDA LEADLQAALP QVWGRRVHSV FLGGGTPSLL SAAGLDRLLT LLRTLLPLDP
     LAEITLEANP GTVEAARFRD YRAAGVNRLS LGIQSFNDRF LAAIGRIHGG DEARAAVDLA
     LATFDRVNID LMYALPGQDM AHALVDLRTA IASGAGHLSC YHLTLEPNTP FAHEPPALPD
     DEVAADMQDA IEAELAAAGF THYETSAFAR TAQQCRHNLN YWTFGDYLGI GPGAHGKLSS
     HQGIVREMRH KHPEHYLAAA ARGDFVHLRH TVGAADLPFE FMMNALRLCD GVPAALFTAR
     TGLPLAAIGE ALATARSAGL LDADPATLRP TARGQRFLND LLQRFLPDS
//
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