ID A0A0F6QZ67_9CORY Unreviewed; 302 AA.
AC A0A0F6QZ67;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024,
GN ECO:0000313|EMBL:AKE40967.1};
GN ORFNames=UL82_03805 {ECO:0000313|EMBL:AKE40967.1};
OS Corynebacterium kutscheri.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE40967.1, ECO:0000313|Proteomes:UP000033457};
RN [1] {ECO:0000313|EMBL:AKE40967.1, ECO:0000313|Proteomes:UP000033457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE40967.1,
RC ECO:0000313|Proteomes:UP000033457};
RX PubMed=26021937;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a
RT Corynebacterial Type Strain with Remarkably Low G+C Content of Chromosomal
RT DNA.";
RL Genome Announc. 3:e00571-15(2015).
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|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|HAMAP-Rule:MF_00024}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_00024}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CobD/CbiB family.
CC {ECO:0000256|ARBA:ARBA00006263, ECO:0000256|HAMAP-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; CP011312; AKE40967.1; -; Genomic_DNA.
DR RefSeq; WP_046439076.1; NZ_LR134381.1.
DR AlphaFoldDB; A0A0F6QZ67; -.
DR STRING; 35755.UL82_03805; -.
DR KEGG; cku:UL82_03805; -.
DR HOGENOM; CLU_054212_1_2_11; -.
DR OrthoDB; 9811967at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000033457; Chromosome.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR NCBIfam; TIGR00380; cobal_cbiB; 1.
DR PANTHER; PTHR34308; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR PANTHER; PTHR34308:SF1; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR Pfam; PF03186; CobD_Cbib; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00024}; Ligase {ECO:0000313|EMBL:AKE40967.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00024};
KW Reference proteome {ECO:0000313|Proteomes:UP000033457};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00024}.
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ SEQUENCE 302 AA; 32792 MW; 9C6A9DCA5A9DEB0E CRC64;
MPHSIMIGMA ADRILGDPHT PWHPVALFGR FAATVEKRTY SDHKVAGVFY TAVCVIPPTA
LSIWAYRRFP EFSTALALYI AVGGTTLEKT GERMHKALEV DDIDAARALV PWLCSRDPQL
LDEAGIVRAT VESLAENTSD AAIAPLVWAG IGGAPLVVLH RVVNTLDAMV GYKNQRYQEF
GWTAARLDDL LGYFPARLTA LIHTVTANEH IQDAVRAWRE DAPRHPSPNA GPVEATAAAH
LGVSLGGKTR YAYGVEMRPI LGTGPAPTIE TITQAVKLAR TTQIIAAGVA MGLRGLRRYR
RI
//