ID K0B8Z0_9ARCH Unreviewed; 279 AA.
AC K0B8Z0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000256|ARBA:ARBA00014921, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=NSED_00585 {ECO:0000313|EMBL:AFS81929.1};
OS Candidatus Nitrosopumilus sediminis.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=1229909 {ECO:0000313|EMBL:AFS81929.1, ECO:0000313|Proteomes:UP000006100};
RN [1] {ECO:0000313|EMBL:AFS81929.1, ECO:0000313|Proteomes:UP000006100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR2 {ECO:0000313|EMBL:AFS81929.1,
RC ECO:0000313|Proteomes:UP000006100};
RX PubMed=23209211; DOI=10.1128/JB.01869-12;
RA Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Ghai R.,
RA Martin-Cuadrado A.B., Rodriguez-Valera F., Rhee S.K.;
RT "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT Nitrosopumilus sediminis" AR2, from Svalbard in the Arctic Circle.";
RL J. Bacteriol. 194:6948-6949(2012).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00028}.
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DR EMBL; CP003843; AFS81929.1; -; Genomic_DNA.
DR RefSeq; WP_014964301.1; NC_018656.1.
DR AlphaFoldDB; K0B8Z0; -.
DR STRING; 1229909.NSED_00585; -.
DR GeneID; 13697988; -.
DR KEGG; nir:NSED_00585; -.
DR PATRIC; fig|1229909.8.peg.124; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_0_0_2; -.
DR OrthoDB; 53136at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006100; Chromosome.
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-KW.
DR CDD; cd05389; CobQ_N; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 4..226
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 279 AA; 31007 MW; 56089AD4F005C8A2 CRC64;
MKSLMIQGTS SGAGKTTLVA ALCRIFSDKG YTVAPFKSQN MSNFAYITPE FEISRAQAIQ
AIGARCKITT DLNPILLKPM GNYDSIVYLN GKRYKKMHAK EYYEEFVNSE GIRMATKSLK
TLQKNFDLVI LEGAGSPAEI NLQKFDIANM KIAQKANASV LLVSDVDKGG AFASLVGTMA
LIEKKYQKLV KGFIFNKFRG DLDVLKPGFQ KLKKITKKPV LGTIPLMILD LPEEDSLNAN
PKEILWTKKN ISKIDNELDK LAKTVKSNIA IKDIEKMLQ
//
