COBQ_HYPNA
ID COBQ_HYPNA Reviewed; 495 AA.
AC Q0C077;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=HNE_2169;
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444;
RX PubMed=16980487; DOI=10.1128/jb.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(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: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; CP000158; ABI77420.1; -; Genomic_DNA.
DR RefSeq; WP_011647164.1; NC_008358.1.
DR AlphaFoldDB; Q0C077; -.
DR SMR; Q0C077; -.
DR STRING; 228405.HNE_2169; -.
DR EnsemblBacteria; ABI77420; ABI77420; HNE_2169.
DR KEGG; hne:HNE_2169; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001959; 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; 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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332342"
FT DOMAIN 252..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 51894 MW; 214C293977FD0A38 CRC64;
MTARAIMIQG TGSDVGKSLL VAGFCRLAAR RGLSVAPFKP QNMSNNAAAT ADGGEIGRAQ
ALQARACGLD PQTDFNPVLL KPQSDCTAQV IVHGRPTATL EAADYMARRD TLRGAVLESF
ARLTARFDLV IVEGAGSPAE INLRDRDIAN MGFARAAGVP VVLAGDIDRG GVIAALVGTK
TVIDPADAAM IRAFLINKFR GDPALFEPAM ADIERMTGWA GLGIVPWLSA AARLPAEDGV
ALEQMRPTGG GRIRIAAPML SRIANFDDAD PLRAEPSVDF FFVPPGQAIP RDVDVILLFG
TKSTLGDMAF LRAQGWDHDI LAHARTGGRI LGICGGYQML GQWLCDPEGV DGAAGELPGL
GLLKTDTTMQ GEKTVRPVTG QCARTGLPVS GYEIHAGLTR GPDAARPFLH LPEGPDGAIS
PDGRVEGTYV HGLFAQDAFR AAWLENVRAG ASSDAAYGAS VEAALDELAD GLEAHLDVDR
FFALAAAPGW RGAPS