ID Q18KB9_HALWD Unreviewed; 594 AA.
AC Q18KB9;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000256|ARBA:ARBA00014921, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cbiP {ECO:0000313|EMBL:CAJ51532.1};
GN Synonyms=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN ECO:0000313|EMBL:CAJ51532.1};
GN OrderedLocusNames=HQ_1404A {ECO:0000313|EMBL:CAJ51532.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51532.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ51532.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180088; CAJ51532.1; -; Genomic_DNA.
DR RefSeq; WP_011570687.1; NC_008212.1.
DR AlphaFoldDB; Q18KB9; -.
DR STRING; 362976.HQ_1404A; -.
DR GeneID; 4193808; -.
DR KEGG; hwa:HQ_1404A; -.
DR eggNOG; arCOG00105; Archaea.
DR HOGENOM; CLU_019250_2_2_2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001975; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; 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; 2.
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}; Ligase {ECO:0000313|EMBL:CAJ51532.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001975}.
FT DOMAIN 9..276
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 309..541
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 56..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 534
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 594 AA; 62945 MW; 00AF9C593BD327FE CRC64;
MSERSTPTIL VAGTASHVGK STVVTGLCRR FANADVRVAP FKAQNMSNEA RAVVRPTADT
DMKSVTADEN DSTAVNSSEQ EETNTITAGV LNSELNPTYG EIGVSQSVQA QAAGVQSVTD
HNPVLLKPRG DAESQLIIDG VAVGHYTAES FYAEHWEQAR SAAVTAHTRL AADHDVIIAE
GAGSIAEINF HDHDLANIET ARFTDARIII VADIERGGVF ASIIGTLELL PDDVRNQVIG
IVITKFRGDK SLLAPGIQTI EDRTGIPVLS VIPYDDPGLP AEDSVSLPAV GERSVRGADD
DAPAEQTVTV AVPRLPRASN TADLDPLAAV PGVRVAFVPL DVSLSRADID AVVITGTKNT
VDDLRALRAS GFDDELREFE GPIVGLCGGY QLLGERLTAI HVEETDSNEK TEIEPAPSND
SNDDDSGHQT LSGLGILPVE TQFSPTKRVA PVTWTLDGFG PLADATGMVT GYEIHAGQTT
ACGPVQTPFE SLTTERIEST DNTADLSQGM TNHHSRDPVA LGAATDSVIG TYLHGLFDNE
AVCEAFVESV FSAANTDRPD IDTTSRSDPY ERAAHLVSSI SFESILGHPL TELK
//
