ID A0A255ZFT9_9BURK Unreviewed; 533 AA.
AC A0A255ZFT9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=CHU94_13415 {ECO:0000313|EMBL:OYQ40292.1};
OS Rhodoferax sp. TH121.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2022803 {ECO:0000313|EMBL:OYQ40292.1, ECO:0000313|Proteomes:UP000216607};
RN [1] {ECO:0000313|EMBL:OYQ40292.1, ECO:0000313|Proteomes:UP000216607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH121 {ECO:0000313|EMBL:OYQ40292.1,
RC ECO:0000313|Proteomes:UP000216607};
RA Cai H.;
RT "Rhodoferax cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) 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:OYQ40292.1}.
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DR EMBL; NOXW01000021; OYQ40292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255ZFT9; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000216607; 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:UP000216607}.
FT DOMAIN 6..229
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 256..490
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 484
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 533 AA; 55975 MW; EBAC0A3909DD1201 CRC64;
MTAKCIMVLG TTSGAGKSWL TTALCRYYAR QGLRVAPFKA QNMSNNARVV ASASGQGEIG
AAQYFQALAA NVVPDVRMNP LLLKPERDTH SQVVLMGQVN LELSAMPWRG RSLKVWPQIA
AALDALRAEN DVVVIEGAGS PAEINLAASD IVNMRVAQHG DAACLLVTDI DRGGAFAHLY
GTWALLPEDQ RPFIKGFVLN KFRGDAALLA PAPQMLQDLT GVPTVATLPM WWQHGLPEED
GVFDDRSVAK GAVRLTVAVI AYPRISNLDE FQPLKNIPGL KLQWVRSPSE LAGLKATDWV
ILPGSKHTSG DLAWLRSQGL DAAIAKHAGQ GGAVLGICGG LQMLGEALID AHGIDGNAPG
LGLLPLVTVF AQDKTVRHTS TAFLSSFRSH ADGGQAADLI LPNAQKSAPG LPPIGVDPGV
PALRPEASPW AALAGVSVTG YEIHHGQTAP HAAMAAAGNA PIAVLPDDLG WTNPQGNVLG
LYLHGMFEDA AVLQALFGAQ LGGTVPTLET VFDGLADFVA ENFAPGVLQG LLR
//
