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Database: UniProt
Entry: A0A0F5PF23_9SPHN
LinkDB: A0A0F5PF23_9SPHN
Original site: A0A0F5PF23_9SPHN 
ID   A0A0F5PF23_9SPHN        Unreviewed;       175 AA.
AC   A0A0F5PF23;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Molybdenum cofactor biosynthesis protein B {ECO:0000256|ARBA:ARBA00015262, ECO:0000256|PIRNR:PIRNR006443};
GN   ORFNames=WP12_05115 {ECO:0000313|EMBL:KKC27067.1};
OS   Sphingomonas sp. SRS2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC27067.1, ECO:0000313|Proteomes:UP000033680};
RN   [1] {ECO:0000313|EMBL:KKC27067.1, ECO:0000313|Proteomes:UP000033680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS2 {ECO:0000313|EMBL:KKC27067.1,
RC   ECO:0000313|Proteomes:UP000033680};
RA   Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT   "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT   isolated from an agricultural field in the United Kingdom.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC       {ECO:0000256|PIRNR:PIRNR006443}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|PIRNR:PIRNR006443}.
CC   -!- SIMILARITY: Belongs to the MoaB/Mog family.
CC       {ECO:0000256|ARBA:ARBA00006112, ECO:0000256|PIRNR:PIRNR006443}.
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:KKC27067.1}.
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DR   EMBL; LARW01000059; KKC27067.1; -; Genomic_DNA.
DR   RefSeq; WP_046192687.1; NZ_LARW01000059.1.
DR   AlphaFoldDB; A0A0F5PF23; -.
DR   STRING; 133190.WP12_05115; -.
DR   PATRIC; fig|133190.4.peg.2854; -.
DR   OrthoDB; 9784492at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000033680; Unassembled WGS sequence.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR012245; MoaB.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR013484; MoaB_proteobac.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   NCBIfam; TIGR02667; moaB_proteo; 1.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR43232; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN B; 1.
DR   PANTHER; PTHR43232:SF2; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN B; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   PIRSF; PIRSF006443; MoaB; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|PIRNR:PIRNR006443};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033680}.
FT   DOMAIN          15..159
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   175 AA;  19313 MW;  5AF434C4A4ABA7B2 CRC64;
     MPIKEDLPFH PVCIAVLTVS DSRDLSQDRS GDTLVMRIEG AGHILADRAI VKDDVELITA
     RLHGWIDDPQ VDCVITTGGT GVTGRDVTPE ALRQVWDKEI PGFGELFRWL SYAKIGTSTI
     QSRATACVAR GTYIFALPGS TGAVKDGWDD ILVHQLDSRH MPCNFVELMP RLLER
//
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