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Database: UniProt
Entry: A0A1T0CH50_9GAMM
LinkDB: A0A1T0CH50_9GAMM
Original site: A0A1T0CH50_9GAMM 
ID   A0A1T0CH50_9GAMM        Unreviewed;       377 AA.
AC   A0A1T0CH50;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thiamine biosynthesis protein ThiH {ECO:0000313|EMBL:OOS21686.1};
GN   ORFNames=B0682_03310 {ECO:0000313|EMBL:OOS21686.1};
OS   Moraxella lincolnii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=90241 {ECO:0000313|EMBL:OOS21686.1, ECO:0000313|Proteomes:UP000191094};
RN   [1] {ECO:0000313|EMBL:OOS21686.1, ECO:0000313|Proteomes:UP000191094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 9405 {ECO:0000313|EMBL:OOS21686.1,
RC   ECO:0000313|Proteomes:UP000191094};
RA   Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA   Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA   Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome sequence of Moraxella lincolnii CCUG 9405T type strain.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:OOS21686.1}.
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DR   EMBL; MUYT01000004; OOS21686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T0CH50; -.
DR   STRING; 90241.B0682_03310; -.
DR   OrthoDB; 9801120at2; -.
DR   Proteomes; UP000191094; 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; SFLDS00029; Radical_SAM; 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:UP000191094};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          257..365
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
SQ   SEQUENCE   377 AA;  42872 MW;  7E6E261680D9C44B CRC64;
     MTFSTHLDTL NWDEICLSIY GKTDHDVKIA LTKDKPDMND LMALLSPAAS QYLEAMAVKA
     QRITRQRFGN TVGLFIPMYL SNLCANECTY CGFSLSNPMT RKTLTHNEIV AECQTINRLG
     FSQVLLVTGE YPSQVGMPYF KTHIKTVREH VSSLLMEVQP LSTDDYAQLK SWGLDGVMLY
     QETYHKPSYA YHHLKGKKRN FNWRLDAPDR IGQAKIDKIG LGVLVGLSDN FRTDCYMMAE
     HLRYLQKTHW QSRFSVAVPR LRPCAGGISP HCTMSDKELV QVLCALRLFA PEVDIVLSTR
     ESPTFRDHVI PLMVTQMSAY SQTKPGGYSA ADNQTADDTL EQFSIDDDRH PKAVVRKLTE
     QGLQPIWKDW DSYLGRE
//
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