ID L9ZFH7_9EURY Unreviewed; 530 AA.
AC L9ZFH7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=C484_21678 {ECO:0000313|EMBL:ELY84801.1};
OS Natrialba taiwanensis DSM 12281.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1230458 {ECO:0000313|EMBL:ELY84801.1, ECO:0000313|Proteomes:UP000011648};
RN [1] {ECO:0000313|EMBL:ELY84801.1, ECO:0000313|Proteomes:UP000011648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12281 {ECO:0000313|EMBL:ELY84801.1,
RC ECO:0000313|Proteomes:UP000011648};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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|PROSITE-ProRule:PRU00605}.
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:ELY84801.1}.
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DR EMBL; AOIL01000070; ELY84801.1; -; Genomic_DNA.
DR RefSeq; WP_006827889.1; NZ_AOIL01000070.1.
DR AlphaFoldDB; L9ZFH7; -.
DR STRING; 1230458.C484_21678; -.
DR PATRIC; fig|1230458.4.peg.4371; -.
DR OrthoDB; 53136at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000011648; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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 6..253
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 286..475
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 369
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 469
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 530 AA; 55753 MW; 4091FEA47CC6E489 CRC64;
MTRTLLVAGT ASHVGKSTVV AGLCRLLADR GVSVAPFKAQ NMSNNARVVV REAGEDSGNP
SAVTAEANSN EADNRWGEIG VSQFTQARAA RLTPTTDCNP VLLKPRGDGE SQLVVQGRAR
EHVPAGSYYE NHWEDARVAA EKSYRRLAAD HDVIVAEGAG SIAEINLHDR DLANVETARF
ADADILLLVD IERGGAFASL YGTIELLPDD IRERVVGALI TKFRGDPSLL DPGIEEIESR
TGVPILGVLP YDDPGLPEED SVGLPGIEER GVRGDDDGVP GEQRLRIAVP RLPRISNATD
LEALAAEPGV SVVYVPIDDG ASDTPLDAVA ADAVVLPGTK NTVDDLRALH AAEFGDALHA
FDGPIVGICG GYQLLGERLT NASLEGTGTD DTLDGLGLLP VETRFDENKR LEQTTVPVDG
SATPLLAGVD GTASGYEIHA GRTRALEPVQ RPLGDASAAR GQVLGTYLHG VFDNTGVRTA
FLDAVARSAG VELPAHDANL SGETATAPAD RAATLLRQHV DAAFLESIRP
//
