ID   COBDQ_LEPIN             Reviewed;         863 AA.
AC   Q8EXQ7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Adenosylcobalamin biosynthesis bifunctional protein CobDQ;
DE   Includes:
DE     RecName: Full=Putative threonine-phosphate decarboxylase;
DE              EC=4.1.1.81;
DE     AltName: Full=L-threonine-O-3-phosphate decarboxylase;
DE   Includes:
DE     RecName: Full=Cobyric acid synthase;
GN   Name=cobDQ; OrderedLocusNames=LB_151;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Zhong Y., Zheng H.-J., Wang S.-Y., Guo X.-K., Zhao G.-P.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       adenosylcobalamin biosynthesis: decarboxylates L-threonine-O-3-
CC       phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor
CC       for the linkage between the nucleotide loop and the corrin ring in
CC       cobalamin, and 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 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + O-phospho-L-threonine = (R)-1-aminopropan-2-yl
CC         phosphate + CO2; Xref=Rhea:RHEA:11492, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58563, ChEBI:CHEBI:58675; EC=4.1.1.81;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class-II
CC       pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the CobB/CobQ family.
CC       CobQ subfamily. {ECO:0000305}.
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DR   EMBL; AE010301; AAN51710.2; -; Genomic_DNA.
DR   RefSeq; NP_714695.2; NC_004343.2.
DR   RefSeq; WP_001052877.1; NC_004343.2.
DR   AlphaFoldDB; Q8EXQ7; -.
DR   SMR; Q8EXQ7; -.
DR   STRING; 189518.LB_151; -.
DR   EnsemblBacteria; AAN51710; AAN51710; LB_151.
DR   KEGG; lil:LB_151; -.
DR   PATRIC; fig|189518.3.peg.4479; -.
DR   HOGENOM; CLU_013947_2_1_12; -.
DR   InParanoid; Q8EXQ7; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001408; Chromosome II.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; 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   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Lyase;
KW   Multifunctional enzyme; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..863
FT                   /note="Adenosylcobalamin biosynthesis bifunctional protein
FT                   CobDQ"
FT                   /id="PRO_0000141305"
FT   DOMAIN          622..810
FT                   /note="GATase cobBQ-type"
FT   REGION          1..373
FT                   /note="Putative threonine-phosphate decarboxylase"
FT   REGION          374..863
FT                   /note="Cobyric acid synthase"
FT   ACT_SITE        704
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        802
FT                   /evidence="ECO:0000250"
FT   BINDING         6..7
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         30
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         159
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         323
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         337
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
SQ   SEQUENCE   863 AA;  97457 MW;  40710C6DC23E055E CRC64;
     MNLPEHGGNL IELSKKAGCN PKEILDFSAN INPLGFPEWL RPFLHSKIED LISYPDPNYT
     SLKKKIHSKY GICTEQIVLG NGASELILQI PFVVQADYAL IAVPCYSGYK EAISLLKIPC
     IEVTLKEEKQ FRLDINELRD VLKSKPDQKA LVFLGHPNNP TGVTLDKIEV LKIVQEFQNS
     VFVIDESFIH FCTNESSFLK DKTENMILIQ SMTKILALPG LRIGICYASP LICSNISKRL
     PTWNVNSIAA SVYEKAISDE DYIENSKQNI KIWKEKLIYD LSNLEFLNLF SSEANFILIK
     ILDNKNIFDL TQELLIKYKI AVRNCENFSG LSKNFIRIAV RTPEENKKII DAFSNIFYGT
     RQRLKSRKKT PSIMFQGTAS NVGKSILTAA LCRILSQDGI KVAPFKSQNM ALNSFVTLNG
     EEIGRAQALQ AQAAKILPDI RMNPILLKPS NEKDSQVIIN GKPLNSMNFK DYDQYKPIAF
     EEVKKSYDSL ASEYNVIIIE GAGSASEVNL KKNDIVNMKM AEYAKADVLL VGNIDHGGLF
     GSLLGTMETL TEWERKLVFG FIINRFRGAK ELLKTGINYI EEYTNKPILG IVPYIKNLKL
     PEEDSLEFKS GALDDTSKLE ERLDVVLIDI PRISNHTDID ALRAEPDVRV RIVRTVEDLG
     EPDVLILPGS KNVISDLNHL YDVGLVNKIF ALSRNQKTDI VGICGGYQML GKNIFDPYRI
     ESDQGSIQGI SLLQIETILE KNKSLKRVFA THIPTKTEVE GYEIHHGKTK SIGNTRVILL
     NEKAEELGHS DPTGRIWGTY IHGIFDKDEF RRKYLDQIRI RKGKSPLVKV QVSYNLEKSL
     DRLARYVRQS LNINLIYRKL GLG