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 08-NOV-2023, entry version 113.
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; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC 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 PaxDb; 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 OrthoDB; 9808302at2; -.
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; 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; 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
//
