ACI_VIBSJ
ID ACI_VIBSJ Reviewed; 362 AA.
AC H2IFX0;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=3,6-anhydro-alpha-L-galactonate cycloisomerase {ECO:0000305};
DE Short=AHGA cycloisomerase {ECO:0000303|PubMed:25156229};
DE EC=5.5.1.25 {ECO:0000269|PubMed:25156229};
GN Name=Vejaci {ECO:0000303|PubMed:25156229};
GN ORFNames=VEJY3_09370 {ECO:0000312|EMBL:AEX22356.1};
OS Vibrio sp. (strain EJY3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1116375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EJY3;
RX PubMed=22535948; DOI=10.1128/jb.00303-12;
RA Roh H., Yun E.J., Lee S., Ko H.J., Kim S., Kim B.Y., Song H., Lim K.I.,
RA Kim K.H., Choi I.G.;
RT "Genome sequence of Vibrio sp. strain EJY3, an agarolytic marine bacterium
RT metabolizing 3,6-anhydro-L-galactose as a sole carbon source.";
RL J. Bacteriol. 194:2773-2774(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=EJY3;
RX PubMed=25156229; DOI=10.1111/1462-2920.12607;
RA Yun E.J., Lee S., Kim H.T., Pelton J.G., Kim S., Ko H.J., Choi I.G.,
RA Kim K.H.;
RT "The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component
RT of red macroalgae, in a marine bacterium.";
RL Environ. Microbiol. 17:1677-1688(2015).
CC -!- FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which
CC is the major monomeric sugar of red macroalgae. Catalyzes the
CC isomerization of 3,6-anhydrogalactonate (AHGA) to 2-keto-3-deoxy-
CC galactonate (KDGal). {ECO:0000269|PubMed:25156229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,6-anhydro-L-galactonate = 2-dehydro-3-deoxy-L-galactonate;
CC Xref=Rhea:RHEA:21512, ChEBI:CHEBI:75545, ChEBI:CHEBI:83435;
CC EC=5.5.1.25; Evidence={ECO:0000269|PubMed:25156229};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8ZL58};
CC -!- BIOTECHNOLOGY: Could be used for bioconversion of red macroalgal
CC biomass into biofuels or industrial chemicals.
CC {ECO:0000305|PubMed:25156229}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; CP003241; AEX22356.1; -; Genomic_DNA.
DR RefSeq; WP_014232231.1; NC_016613.1.
DR PDB; 5XD7; X-ray; 2.20 A; A=1-362.
DR PDB; 5XD8; X-ray; 2.50 A; A/B=1-362.
DR PDB; 5XD9; X-ray; 2.60 A; A=1-362.
DR PDBsum; 5XD7; -.
DR PDBsum; 5XD8; -.
DR PDBsum; 5XD9; -.
DR AlphaFoldDB; H2IFX0; -.
DR SMR; H2IFX0; -.
DR KEGG; vej:VEJY3_09370; -.
DR PATRIC; fig|1116375.3.peg.1874; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_3_1_6; -.
DR BioCyc; MetaCyc:MON-18903; -.
DR BRENDA; 5.5.1.25; 6640.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019388; P:galactose catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034382; AHGA_cycloisomerase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00557; 3_6-anhydro-alpha-L-galactonat; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Magnesium; Metal-binding.
FT CHAIN 1..362
FT /note="3,6-anhydro-alpha-L-galactonate cycloisomerase"
FT /id="PRO_0000432213"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8ZL58"
FT ACT_SITE 300
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8ZL58"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8ZL58"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8ZL58"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8ZL58"
FT STRAND 4..21
FT /evidence="ECO:0007829|PDB:5XD7"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5XD8"
FT STRAND 29..41
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 46..57
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 100..120
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:5XD7"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5XD8"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:5XD8"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5XD8"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:5XD7"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:5XD8"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5XD7"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:5XD7"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5XD7"
SQ SEQUENCE 362 AA; 40448 MW; F652FAAAC6947143 CRC64;
MKTTIKDIKT RLFKIPLKEI LSDAKHGDHD HFELITTTVT LEDGSQGTGY TYTGGKGGYS
IKAMLEYDIQ PALIGKDATQ IEEIYDFMEW HIHYVGRGGI STFAMSAVDI ALWDLKGKRE
GLPLWKMAGG KNNTCKAYCG GIDLQFPLEK LLNNICGYLE SGFNAVKIKI GRENMQEDID
RIKAVRELIG PDITFMIDAN YSLTVEQAIK LSKAVEQYDI TWFEEPTLPD DYKGFAEIAD
NTAIPLAMGE NLHTIHEFGY AMDQAKLGYC QPDASNCGGI TGWLKAADLI TEHNIPVCTH
GMQELHVSLV SAFDTGWLEV HSFPIDEYTK RPLVVENFRA VASNEPGIGV EFDWDKIAQY
EV
