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Database: UniProt
Entry: T0FQU5_9LEPT
LinkDB: T0FQU5_9LEPT
Original site: T0FQU5_9LEPT 
ID   T0FQU5_9LEPT            Unreviewed;       863 AA.
AC   T0FQU5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:EQA71960.1};
GN   ORFNames=LEP1GSC059_1144 {ECO:0000313|EMBL:EQA71960.1};
OS   Leptospira noguchii serovar Panama str. CZ214.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1001595 {ECO:0000313|EMBL:EQA71960.1, ECO:0000313|Proteomes:UP000015442};
RN   [1] {ECO:0000313|EMBL:EQA71960.1, ECO:0000313|Proteomes:UP000015442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CZ214 {ECO:0000313|EMBL:EQA71960.1,
RC   ECO:0000313|Proteomes:UP000015442};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   Fouts D.E.;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC       adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC       and one molecule of ATP is hydrogenolyzed for each amidation.
CC       {ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00028}.
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:EQA71960.1}.
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DR   EMBL; AKWY02000020; EQA71960.1; -; Genomic_DNA.
DR   RefSeq; WP_017213327.1; NZ_AKWY02000020.1.
DR   AlphaFoldDB; T0FQU5; -.
DR   GeneID; 23202018; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000015442; Unassembled WGS sequence.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00609; AAT_like; 1.
DR   CDD; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR033949; CobQ_GATase1.
DR   InterPro; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00028};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00028}; Ligase {ECO:0000313|EMBL:EQA71960.1}.
FT   DOMAIN          23..352
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   DOMAIN          373..604
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          624..809
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        704
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        802
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   863 AA;  97392 MW;  ED76A8948EA06C50 CRC64;
     MNLFEHGGNL IELSKRVGCN PKEILDFSAN INPLGFPEWL RPFLHSKIED LISYPDPNYT
     SLKNKIHSKY KICSDQIVIG NGASELILQI PFVVKADYTL IAVPCYSGYK EAVSLRKIPC
     VEVILKEEKQ FRLDIDEVRD VLKSKINQKA LIFLGHPNNP TGVTLDKIEI LKLAQEFQNS
     IFVIDESFIH FCTKGSSFLK DRTENMILIQ SMTKILALPG LRIGICYASS SICSNISKKL
     PTWNVNSLAA SVYEKAIDDE NYIKNSKQNM QVWKEKLIYD LSNLEFLNPF PSDTNFILIK
     ILGNRNISNL VQELLLKYKI AVRNCENFSG LSKNFIRIAV RIPEENEKII DAFSNIFYGT
     RQKLKFSKKT PSIMFQGTAS NVGKSILTAA LCRILAQDGI KVAPFKSQNM ALNSFVTLNG
     EEIGRAQALQ AQAAKILPDV RMNPILLKPS SEKKSQVIIN GKVINSMNFK NYDQYKSIAF
     EEVKKSYDSL SSEYNVIIIE GAGSASEVNL KKNDIVNMRM AEYAKADVLL VGNIDHGGLF
     GSILGTMETL TEWERKLVFG FVINRFRGIK ELLKTGINYI EDYTNRPVIG IVPYIKNLEL
     PEEDSLEFKS RALYDTSMLG DRLDVVLIDI PRISNHTDID ALKAEPDVRV RIVRTAEDLG
     EPDILILPGS KNVISDLNHL YDVGLADKIF ALSRNQKTDI VGICGGYQML GKNIFDPYCI
     ESNQGHIQGI SLLPIETILE KIKSIKRVFA THIPTKTEVE GYEIHHGKTK SVGNTHVILL
     NEKSEELGHS DSTGRIWGTY IHGIFDKDQF RRKYLDQIRI RKGKAPLVDV QVSYNLEKSL
     DKLAKHVRRS LNINLIYRKL GLS
//
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