COBQ_HALHL
ID COBQ_HALHL Reviewed; 483 AA.
AC A1WYA9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Hhal_1907;
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-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: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; CP000544; ABM62671.1; -; Genomic_DNA.
DR AlphaFoldDB; A1WYA9; -.
DR SMR; A1WYA9; -.
DR STRING; 349124.Hhal_1907; -.
DR EnsemblBacteria; ABM62671; ABM62671; Hhal_1907.
DR KEGG; hha:Hhal_1907; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000647; 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; 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; 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; 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..483
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002359"
FT DOMAIN 252..430
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 422
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 483 AA; 51459 MW; 536DB4E8A7732652 CRC64;
MVRARTLMLQ GTCSGAGKTA LVAGLCRLLA RHGVRVAPFK PQNMSNNAAV TADGGEIGRG
QWLQALAAGL PAHTDMNPVL LKPEAERTAQ VVVQGHVTGR LEARAFREAR QPLLPPVLES
FQRLCAAYDV VLVEGAGSPA EPNLRQGDIA NMGFAEAADV PVWLVGDIDR GGVFASLLGT
LEWLDDADRR RVEALIINRF RGSPELLGEA PAQLEARGGV PVIGVVPAVP DLHLPEEDAP
YRMAGPRGSG GALQVVAVAY PRMSNHDDLD ALDAESGVHV RFARQPRELD GADLIVLPGS
KHVFSDLAWL RESGMAEALY RHCRYGGRVV GLCGGLQMLG EGIEDPEGVE GGGSAPGLGL
LPVHTRLAPT KQLAEVHGHA EWPAPVAVTG YEIHHGVTGA QEGLFPFVAR SDDGRVLGSY
LHRLFDSGPF RRALLVEWFA LEGEGGDEQA RIEAELDRLA DTLEQALEPG WLKALGVPAR
PST
