ID K8XH34_RHOOP Unreviewed; 512 AA.
AC K8XH34;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=WSS_A20659 {ECO:0000313|EMBL:EKT80709.1};
OS Rhodococcus opacus M213.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1129896 {ECO:0000313|EMBL:EKT80709.1, ECO:0000313|Proteomes:UP000005951};
RN [1] {ECO:0000313|EMBL:EKT80709.1, ECO:0000313|Proteomes:UP000005951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M213 {ECO:0000313|EMBL:EKT80709.1,
RC ECO:0000313|Proteomes:UP000005951};
RX PubMed=23409266;
RA Pathak A., Green S.J., Ogram A., Chauhan A.;
RT "Draft Genome Sequence of Rhodococcus opacus Strain M213 Shows a Diverse
RT Catabolic Potential.";
RL Genome Announc. 1:E00144-12(2013).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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:EKT80709.1}.
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DR EMBL; AJYC02000066; EKT80709.1; -; Genomic_DNA.
DR RefSeq; WP_005259294.1; NZ_AJYC02000066.1.
DR AlphaFoldDB; K8XH34; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000005951; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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}.
FT DOMAIN 11..236
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 264..441
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 512 AA; 53711 MW; 83154C411F135868 CRC64;
MSESRWKGAL LVAGTTSDAG KSVLVAGLCR MLARRGVRVA PFKAQNMSNN SVVTLDGGEI
GRAQALQAAA CGLEPSVRFN PVLLKPGSDR TSQLVVRGRA VTSVGARDYI EHRQHLRAVV
AEELASLRAE YDVVICEGAG SPAEINLRAT DLANMGLARA ADLPVVVVGD IDRGGVLAHL
FGTVAVLAPE DQALIAGFVI NKFRGDVSLL GPGLEQLTAM TGRPTLGVIP FAEDLWLDAE
DSLGVVGDAP VGRPAPPIGD DWLRVAAIRL PRISNSTDVE ALACEPGVSV RWVTDPSRLE
DTDLIVLPGS KSTVSDLEWL RRNGIADAIA VHAKRGGPVL GVCGGYQMLG SVIVDDVESG
RGAVPGLGLL DLEIEFAPDK VLAQVRGDAH GVPVSGYEIH HGRVRRNGDQ PLLHAGSGAA
EGSIRGAVYG THWHGLLETD RFRRLLLDDV AEHAGRTGFV TAPDTDVAAI RAAQLDLLAD
LVEQNLDLRA LADLLGAGAP EGLPAIASTL VR
//
