ID A0A0G3H496_9CORY Unreviewed; 193 AA.
AC A0A0G3H496;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Molybdopterin biosynthesis enzyme {ECO:0000313|EMBL:AKK08209.1};
DE EC=4.2.1.96 {ECO:0000313|EMBL:AKK08209.1};
GN Name=moaB {ECO:0000313|EMBL:AKK08209.1};
GN ORFNames=CTEST_03800 {ECO:0000313|EMBL:AKK08209.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08209.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK08209.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08209.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
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DR EMBL; CP011545; AKK08209.1; -; Genomic_DNA.
DR RefSeq; WP_047252602.1; NZ_JAASJB010000007.1.
DR AlphaFoldDB; A0A0G3H496; -.
DR STRING; 136857.CTEST_03800; -.
DR KEGG; cted:CTEST_03800; -.
DR PATRIC; fig|136857.5.peg.750; -.
DR OrthoDB; 9784492at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000035540; Chromosome.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AKK08209.1};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000035540}.
FT DOMAIN 41..182
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 193 AA; 20222 MW; 2E723B365AA3C451 CRC64;
MMISSPDVSR SSTLLDVGEP DEEFLFASEQ EERRKAQRRA LVVLVSDHAI GSGEDTDRVV
AELLVEADFA VDAVVAVKSK KSQIRQAIET GVVGGVDLVL TIGGTGVGPR DKTPEATRVL
LDQMVPGIAQ ALRSSGLACG AVDACTSRGI AGVSGSTVIV NLAASRSAVR DGMATLTPLV
HHLIDQLQKY SVE
//