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
//