ID E1QLQ2_DESB2 Unreviewed; 707 AA.
AC E1QLQ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:ADK86487.1};
GN OrderedLocusNames=Deba_3134 {ECO:0000313|EMBL:ADK86487.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK86487.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK86487.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; CP002085; ADK86487.1; -; Genomic_DNA.
DR RefSeq; WP_013259923.1; NC_014365.1.
DR AlphaFoldDB; E1QLQ2; -.
DR STRING; 644282.Deba_3134; -.
DR KEGG; dbr:Deba_3134; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG2030; Bacteria.
DR eggNOG; COG3255; Bacteria.
DR HOGENOM; CLU_023984_0_0_7; -.
DR OrthoDB; 9802564at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009047; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT DOMAIN 156..264
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT DOMAIN 620..706
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
SQ SEQUENCE 707 AA; 75314 MW; 9562F61D6664100D CRC64;
MALNLDAINK KIGPLTKRYD WKDVALYALG VGAGFDELEY VYEKKLKVIP SFSIASIFNF
LAEVGIKSGL DLSGVLHGGQ ELIFYNPIPI EGELTTEGRI TAMYDLGQGK GATIIAEGDT
FHGDGQKLFK NILTVFARKD GGFGGEAPPK EVFSFPDRPA DFEELAVPSA DQPLIYRLSG
DTFDLHVDPS FAKLAGFEKP IMHGLCTHGY ACRALIKHLF PGQPERLSRF KVRFSRTLYP
GEAIKTQIWK IDDGKALFRV VNAQSGEVVI DRGEAEWLGD AELARRQSLG RINFDGQVAI
VTGAGAGLGR AYALELAKRG AKVVVNDLGG ARDGQGGDTA AADKVVREII EAGGQAVANY
DSVSTPEGGD NIVKTAMDAF GRVDILINNA GILRDRTLVK MEPADWDAVM DVHLGGAYNV
TRPAIKVMRD QAYGRVIFTS SAAGLYGNFG QTNYSAAKMG LVGLMNTLKL EGAKSNINVN
TVAPVAGTRL TEDVMPPDLF QKLAPEFVTP LVLYLCSEQC KASGQIFNAG MGYFNRAAVL
TGPGATVGEE GVFPSLEQVA AKIKDICKMD GAVEFHDLNA SLGPILEAWS PKKPAAGAAS
KAPSVADIFA GMAAAFQADK AAGVEVSFQY VIGGEGGGEW FAEIAGGACK VGQGKHPSPT
TTIKMKAPDF VAMIGGQLNA MAAFTSGKLQ IEGDVMKSQL IEKLFKF
//
