ID   COBQ_HALMA              Reviewed;         492 AA.
AC   Q5V0Z6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=rrnAC1938;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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:0000255|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR   EMBL; AY596297; AAV46807.1; -; Genomic_DNA.
DR   RefSeq; WP_011223936.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V0Z6; -.
DR   STRING; 272569.rrnAC1938; -.
DR   EnsemblBacteria; AAV46807; AAV46807; rrnAC1938.
DR   GeneID; 40152865; -.
DR   KEGG; hma:rrnAC1938; -.
DR   PATRIC; fig|272569.17.peg.2594; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001169; Chromosome I.
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; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 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; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000141345"
FT   DOMAIN          259..443
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   492 AA;  51201 MW;  54D56772D1E09D74 CRC64;
     MAHTLLVAGT ASHVGKSTVA AGLCRYLADC GVSVAPFKAQ NMSNNARATP GGEVGVSQYV
     QARAAGVAPS TDHNPVLLKP RGDGESQLIL DGDAVGHFEA RGYYDEHWED ALETARAAHD
     RLAQSHDVIV AEGAGSIAEI NLHDRDLANI ETARFADADI LLVADIERGG VFASLVGTLE
     LVPDDIRKQV AGAVITKFRG DQSLLDPGID AFEDRTGVPV LGVLPHDDPG LPEEDSVALP
     PVGERSVVGD DDAVPDAESV TVAVPRLPRI SNFTDLQPLA HEPGVRVAYI PPDAALDDAD
     AVVLPGSKNT VDDLRALTDA GFGDRLRSFD GPVVGLCGGY QMLGEAITNA TIEGTGDADR
     VEGLGLLPVT TEFSESKTVE HVQRNIDGVG PLSGASGTVE GYEIHMGDST LTGAAARPFD
     GDGAGTDTVL GTYLHDLFSN DTARDAFVRN TFESAGTVLP AATGRADGDP YERAAGLITD
     HVDLGPLGLS DQ