ID A0A0C9PGX5_9BACT Unreviewed; 525 AA.
AC A0A0C9PGX5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=BROSI_A2707 {ECO:0000313|EMBL:GAN34171.1};
OS Candidatus Brocadia sinica JPN1.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN34171.1, ECO:0000313|Proteomes:UP000032309};
RN [1] {ECO:0000313|EMBL:GAN34171.1, ECO:0000313|Proteomes:UP000032309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPN1 {ECO:0000313|EMBL:GAN34171.1,
RC ECO:0000313|Proteomes:UP000032309};
RA Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT "Candidatus Brocadia sinica".";
RL Genome Announc. 3:e00267-15(2015).
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:GAN34171.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAFN01000001; GAN34171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9PGX5; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000032309; 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:UP000032309}.
FT DOMAIN 1..227
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 271..470
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 236..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 462
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 525 AA; 58003 MW; 419585CF26A1E1C4 CRC64;
MIQGTGSHVG KSILVCALCR ILKQDGYRVA PFKAQNMALN SFVTKDGKEM GRAQVAQAEA
AGIEPMVEMN PILLKPTGDC GSQVVIMGKP IGNMTAREYY QKKGEFISII KGAYDTLRNR
FDIIVIEGAG SPAEINLKDD DIVNMGMAKM ASAPVLLVTD IDRGGAFAWI VGTLELLTAT
ERDRVKGIVF NKFRGDKGIL QPGLDMLENR INKPVLGIIP YIHNLSIDDE DSVSLEYSGN
NDRDQGSGVR GQNTGDKALT PDSRLPASFI DIVVIKLPRI SNFTDFNIFT HGKDVRVRFV
DKAENIGKPD LLIIPGTKNT IGDLIFLEER DISEEIKNLS MCGTMIMGIC GGYQMLGKQI
NDPYHVESAT DSIQGMGLLN TVTTFAREKQ TYQVKASLLD HENLFHVNDE LAGYEIHMGD
TIFNGHKALK PFARITERAG KTVNILDGCV SADGKVLGTY IHGIFDNDEF RLKLMNCLRS
KKGLEPSREC HVGFKSIKEQ RYNKLADIVR ENMDMNTVYN ILKLS
//
