COBQ_THEVB
ID COBQ_THEVB Reviewed; 493 AA.
AC Q8DI74;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=tll1716;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; BA000039; BAC09268.1; -; Genomic_DNA.
DR RefSeq; NP_682506.1; NC_004113.1.
DR RefSeq; WP_011057553.1; NC_004113.1.
DR AlphaFoldDB; Q8DI74; -.
DR SMR; Q8DI74; -.
DR STRING; 197221.22295441; -.
DR PRIDE; Q8DI74; -.
DR EnsemblBacteria; BAC09268; BAC09268; BAC09268.
DR KEGG; tel:tll1716; -.
DR PATRIC; fig|197221.4.peg.1797; -.
DR eggNOG; COG1492; Bacteria.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 HAMAP; MF_00028; CobQ; 1.
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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..493
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141333"
FT DOMAIN 252..441
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 433
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 493 AA; 54282 MW; AC780F0F64DD9F5F CRC64;
MKAKSLMVVG TTSHAGKSLL AAVICRWLAQ QGYRVTPFKG QNMALNAYVT REGGEIGYAQ
AMQAWAAGIE PEVAMNPILL KPQGNMTSQV ILRGQVVGVT RAADYYRDYF ERGWQAITEA
LADLQQRFDW IVCEGAGSPA EINLKHRDLT NMRVATYLGA PTILVADIDR GGVFAHIVGT
LMLLEPAERA LIQGIVINKF RGQRSLLDSG LQWLEETTGV PVLGVIPWLE RHYAAEDSLD
LWDPRPQRQG ADLKITVIRL PRIANFTDID PLLAEPSVAV EFLPPHRPLG RPDAVILPGT
KTTIADLQVL RETGMAEQLK TYAAQGGTIL GICGGWQMLG TAISDPLGLE GCPGTYEGLG
LMPLHTQLGP TKCTQQQQTQ SLYFNCPEPI LGYEIHQGQS EYTGDRQGWH PLFAAPELGL
VNRAGTLWGT YLHGLLENGP WRRHWLNGLR SRRQLPPLPT AIPHYGEQRT VALDELTKTV
MAHLNLRGIC KLC