ID A0A0Q0TWZ1_9CORY Unreviewed; 400 AA.
AC A0A0Q0TWZ1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=UDP-galactopyranose mutase {ECO:0000313|EMBL:KQB83459.1};
DE EC=5.4.99.9 {ECO:0000313|EMBL:KQB83459.1};
GN Name=glf {ECO:0000313|EMBL:KQB83459.1};
GN ORFNames=Clow_02262 {ECO:0000313|EMBL:KQB83459.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB83459.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB83459.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB83459.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000256|ARBA:ARBA00009321}.
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:KQB83459.1}.
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DR EMBL; LKEV01000009; KQB83459.1; -; Genomic_DNA.
DR RefSeq; WP_055179166.1; NZ_LKEV01000009.1.
DR AlphaFoldDB; A0A0Q0TWZ1; -.
DR STRING; 1544413.Clow_02262; -.
DR PATRIC; fig|1544413.3.peg.2264; -.
DR OrthoDB; 9769600at2; -.
DR Proteomes; UP000050488; Unassembled WGS sequence.
DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR InterPro; IPR004379; UDP-GALP_mutase.
DR InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR NCBIfam; TIGR00031; UDP-GALP_mutase; 1.
DR PANTHER; PTHR21197; UDP-GALACTOPYRANOSE MUTASE; 1.
DR PANTHER; PTHR21197:SF0; UDP-GALACTOPYRANOSE MUTASE; 1.
DR Pfam; PF03275; GLF; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KQB83459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488}.
FT DOMAIN 154..366
FT /note="UDP-galactopyranose mutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03275"
SQ SEQUENCE 400 AA; 46069 MW; 2CC804282D291C5C CRC64;
MMQKQYDLIV VGSGLFGLTV AERAASQQGK KVLIVERRSH IGGNAYSEAE PETGIEIHKY
GAHLFHTSNK RVWEYVNQFT EFTGYQHRVF AMHDGTAYQF PMGLGLINQF FGKYYSPEEA
RALIAEQTDG LDPAEATNLE EKAISLIGRP LYEAFIRDYT AKQWQTDPKE LPAGNITRLP
VRYTFDNRYF TDTYEGLPVE GYTAWLERMA AHENIEVRLD TDWFEVREEL RAASPEAPVV
YTGPLDRYFD YAEGHLGWRT LDFEASVEPV GDFQGTPVMN YNDADVPFTR IHEFRHFHPE
RADRYPKDKT VIMKEYSRFA EEGDEPYYPI NTPEDRAKLE AYRRRAAEES KNAKVLFGGR
LGTYQYLDMH MAIGAALSMF DNHLVPFWEE GASLEQSRGH
//