ID Q0F0U5_9PROT Unreviewed; 476 AA.
AC Q0F0U5;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 102.
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=SPV1_11956 {ECO:0000313|EMBL:EAU55446.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU55446.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU55446.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU55446.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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:EAU55446.1}.
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DR EMBL; AATS01000003; EAU55446.1; -; Genomic_DNA.
DR RefSeq; WP_009849909.1; NZ_DS022294.1.
DR AlphaFoldDB; Q0F0U5; -.
DR STRING; 314344.AL013_06635; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_0; -.
DR InParanoid; Q0F0U5; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000005297; 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:UP000005297}.
FT DOMAIN 4..227
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 251..423
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 476 AA; 51291 MW; FB14BA4C5761DC5E CRC64;
MKSLMIQGTA SGVGKSVLVA GLCRLLARNG VRVAPFKPQN MSNNAAVTID GGEIGRAQAL
QAFACGIEPS VHMNPVLIKP EADEQAQLVV RGQVVGQLHA KRFREDRIGW MQMVLESFAL
LQAQYDVVII EGAGSPAEPN LREGDIANMG FAEAADVPVW LVGDIDCGGV FAALTGSLAI
LSDSEQQRVK ALLINRFRGN MELLDDALVW LEEKTGRPVA GVIPWLALEL PEEDAPYRHA
QDSAPDSIQL NIAVIALPRM SNHDDIDPLA SEAGVNLRFV RTTKELNHAD LIILPGSKHV
ASDLAWLRQS GFVPALARHL RYGGNVLGIC GGMQMLGTVI EDDGVEGDSA EGLGWLPLAT
TMRTQKTLIK VDRPSPCFAG ERVTGYEIHH GESDSDKALF PFACKSADGL VWGSYLHGLF
EQGGFRKAWL NELGFSASDG KDQHQRTMDS LDLLADALEQ AIDPELLKPL LAGSSL
//
