ID A0A132BZK9_9RHOB Unreviewed; 488 AA.
AC A0A132BZK9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN ECO:0000313|EMBL:KUP93267.1};
GN ORFNames=TRIHO_18680 {ECO:0000313|EMBL:KUP93267.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP93267.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP93267.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP93267.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-2015) 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|ARBA:ARBA00025166, 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|ARBA:ARBA00006205, 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:KUP93267.1}.
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DR EMBL; LPUY01000055; KUP93267.1; -; Genomic_DNA.
DR RefSeq; WP_068242363.1; NZ_LPUY01000055.1.
DR AlphaFoldDB; A0A132BZK9; -.
DR PATRIC; fig|1768241.3.peg.1962; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000068382; Unassembled WGS sequence.
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-UniRule.
DR CDD; cd05389; CobQ_N; 1.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00313; cobQ; 1.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000068382}.
FT DOMAIN 6..239
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 251..435
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 488 AA; 51491 MW; 989350B11BCB1CE9 CRC64;
MTSKAIMIQG TGSNVGKSLI VAGLARALLR RGLKVAPFKS QNMSNNAAVT ADGGEIGRAQ
ALQARAAGLA PHTDMNPVLL KPETDTGAQV IVQGKRRGTR SAGSFMRDKS GLLEAALESF
HRLAAQYDMI LVEGAGSPAE TNLRQGDIAN MGFAEAADIP VVLVGDIHRG GVIAQIVGTH
TVLDAADRAR IAGFAVNRFR GERSLFDAGR DDIAHRTGWP ALGVIPWFPE AWKLPAEDMM
DIASHAGGAC KIVVPQLERM ANFDDLDPLA AEPDVTVEIV PPGRALPGDA DLVLIPGSKS
TIGDLAYLRA QGWDIDIRAH HRRGGHVIGL CGGYQMLGET ISDPDGVDGR PGKVAGLGLL
DVETVMAGDK RVTLSTAQTC EGGLPVSGYE IHMGRTTGPD CARPWLTLDG RAEGAVSGDG
RVRGSYLHGL FSSDAFRSAF LAELGHSGSA QYDSGVEATL DALADHLERY LDIDRLLAMS
KPVRLPPE
//
