ID A0A1A8T3P7_9GAMM Unreviewed; 494 AA.
AC A0A1A8T3P7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:SBS25693.1};
GN ORFNames=MAQ5080_00337 {ECO:0000313|EMBL:SBS25693.1};
OS Marinomonas aquimarina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=295068 {ECO:0000313|EMBL:SBS25693.1, ECO:0000313|Proteomes:UP000092627};
RN [1] {ECO:0000313|EMBL:SBS25693.1, ECO:0000313|Proteomes:UP000092627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5080 {ECO:0000313|EMBL:SBS25693.1,
RC ECO:0000313|Proteomes:UP000092627};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; FLOC01000001; SBS25693.1; -; Genomic_DNA.
DR RefSeq; WP_067204614.1; NZ_LTAV01000001.1.
DR AlphaFoldDB; A0A1A8T3P7; -.
DR STRING; 295068.MAQ5080_00337; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000092627; 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:UP000092627}.
FT DOMAIN 6..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 254..438
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 432
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 54154 MW; A91281748AC46A51 CRC64;
MRFFNLMVQG TTSDAGKSTL VTALCRLMKE RGVNVAPFKP QNMALNSAVT ADGKEIGRAQ
AVQAYAAGLE PDVHMNPILL KPNTDIGAQV IIQGHSVGNM NAVGYHEYKT IAMNAALDSY
QRLADQYDSV VIEGAGSPAE INLRARDIAN MGFAESIDCP VIIIADIDKG GVFAHLVGTL
ELLSQSEQER VIGFVINRFR GDIALLQSGL DWLEERTGKP VLGVLPYLMG FHLESEDAVA
ASPTKDSSDT KLHVVIPVLP RTSNHTDWDA LRLHPNVQVT LVRKNETIPP ADLVILPGSK
SVQADLAFLR ELGWENYIAR HLRYGGKLLG ICGGFQMLGE FLDDPLGMEN AEPSSAKGLG
YIPMRTELKD GKQLKQRTGV ISPLGNASVK GYEIHSGISE FHQPMQHFAE LENGELEGYL
SEDSQIIGTY LHGLFDDKHA LKALLDWAGA AESQDFDYEA YREQEVARLA KSCDEHMDID
ALIEQCRAFQ AERL
//
