ID A0A160FM40_9BURK Unreviewed; 312 AA.
AC A0A160FM40;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN ORFNames=AYM40_14985 {ECO:0000313|EMBL:ANB73512.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73512.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB73512.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73512.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC aminopropanol on the F carboxylic group. {ECO:0000256|HAMAP-
CC Rule:MF_00024}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00024};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000256|HAMAP-
CC Rule:MF_00024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00024}.
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DR EMBL; CP014578; ANB73512.1; -; Genomic_DNA.
DR RefSeq; WP_063496894.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FM40; -.
DR STRING; 1804984.AYM40_14985; -.
DR KEGG; buz:AYM40_14985; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000076852; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00024; CobD_CbiB; 1.
DR InterPro; IPR031347; AmpE.
DR InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR PANTHER; PTHR38684; PROTEIN AMPE; 1.
DR PANTHER; PTHR38684:SF1; PROTEIN AMPE; 1.
DR Pfam; PF17113; AmpE; 1.
DR Pfam; PF03186; CobD_Cbib; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00024};
KW Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00024};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00024};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00024};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00024}.
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 290..311
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ SEQUENCE 312 AA; 34501 MW; 167DF1D39E21972A CRC64;
MTFFSVLLAL IIEQVRALSP NNPVSALLQY HAESAAHGFD AGKPKHGLLA WLVVVVPWTL
AVALVYYVLY HIHFALAFLW NVAVLYFTLG FRQFSHYFTD IHLALNNDDV PRAREILNEW
TGLDTVDMPV SEIVRHTLIH AVVASHRHVF GVFFWFLIPV GPAGAVLYRI AEYLARAWAR
PVDDRTVAFS SFAQRAFFVI DWVPARLTSL GFAIVGNFED AIYAWRNHAR QWPDANDGVL
LAAGSGALGA RLSGPLAEPS SLDALATGDG GPMQVGDDCT PRTLQSAVGL VWRAVVLWMI
LLLMLTIAVW LA
//
