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Database: UniProt
Entry: V8CBR1_9HELI
LinkDB: V8CBR1_9HELI
Original site: V8CBR1_9HELI 
ID   V8CBR1_9HELI            Unreviewed;       394 AA.
AC   V8CBR1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:ETD24171.1};
GN   ORFNames=HMPREF2086_00920 {ECO:0000313|EMBL:ETD24171.1};
OS   Helicobacter macacae MIT 99-5501.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD24171.1, ECO:0000313|Proteomes:UP000018731};
RN   [1] {ECO:0000313|EMBL:ETD24171.1, ECO:0000313|Proteomes:UP000018731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD24171.1,
RC   ECO:0000313|Proteomes:UP000018731};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species isolated
RT   from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-e00814(2014).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:ETD24171.1}.
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DR   EMBL; AZJI01000004; ETD24171.1; -; Genomic_DNA.
DR   RefSeq; WP_023927644.1; NZ_KI669454.1.
DR   AlphaFoldDB; V8CBR1; -.
DR   STRING; 1357400.HMPREF2086_00920; -.
DR   PATRIC; fig|1357400.3.peg.1266; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_046249_1_0_7; -.
DR   Proteomes; UP000018731; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0009228; P:thiamine 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; IPR010722; BATS_dom.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR012726; ThiH.
DR   InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR   NCBIfam; TIGR02351; thiH; 1.
DR   PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR   PANTHER; PTHR43583:SF1; 2-IMINOACETATE SYNTHASE; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00301; 2-iminoacetate_synthase_(ThiH); 1.
DR   SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR   SMART; SM00876; BATS; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018731};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          271..385
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
FT   REGION          343..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  44344 MW;  20F16D207320BC01 CRC64;
     MVNPSSVWEF QSTMQDIDSN ILECVLEIRE SYNPDAYSSK EVKSALSKHY LDIGDLCALL
     SPAAQPFLEE IATQAQKRVK SYFGNSINVF TPLYLSNHCA SKCVYCGFQK GNKIKRAKLE
     YDEIKAELEI IAKSGLQEVL FLCGEGREYA SVEYIAKSCE LAKQYFKVIG VEIYALNVDE
     YELLHKSGCD FVTLFQETYC PKKYARIHIE GEKRAFAYRF YAQERALRAG MRGVGFGALL
     GIDDFRKDAL SCALHAYFLQ RKYPHAEIAL SIPRLRPIIN NPKIHPKAVT ESRLLQVLCA
     YRLFLPYASI TISSREGARF RNNVIKLGAN KISAGVSVAI GERSAEEKKS RGDDAEKKGD
     EQFSISDNRS VEEILSMLKI AHLQPVMSDS VFVG
//
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