GenomeNet

Database: UniProt
Entry: S9X2R1_CAMFR
LinkDB: S9X2R1_CAMFR
Original site: S9X2R1_CAMFR 
ID   S9X2R1_CAMFR            Unreviewed;       616 AA.
AC   S9X2R1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=MIT domain-containing protein {ECO:0000259|SMART:SM00745};
GN   ORFNames=CB1_000632076 {ECO:0000313|EMBL:EPY82733.1};
OS   Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY82733.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY82733.1, ECO:0000313|Proteomes:UP000030684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX   PubMed=23149746;
RG   Bactrian Camels Genome Sequencing and Analysis Consortium;
RA   Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA   Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA   Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA   Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA   Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA   Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA   Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA   Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA   Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA   Bayaer T., Li Y., Meng H.;
RT   "Genome sequences of wild and domestic bactrian camels.";
RL   Nat. Commun. 3:1202-1202(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH;
CC         Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349;
CC         EC=1.1.1.102; Evidence={ECO:0000256|ARBA:ARBA00024581};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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DR   EMBL; KB016902; EPY82733.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9X2R1; -.
DR   Proteomes; UP000030684; Unassembled WGS sequence.
DR   GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006666; P:3-keto-sphinganine metabolic process; IEA:InterPro.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR   CDD; cd08939; KDSR-like_SDR_c; 1.
DR   CDD; cd02678; MIT_VPS4; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR045022; KDSR-like.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   InterPro; IPR045253; VPS4_MIT.
DR   PANTHER; PTHR43550; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 1.
DR   PANTHER; PTHR43550:SF3; 3-KETODIHYDROSPHINGOSINE REDUCTASE; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00745; MIT; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
FT   DOMAIN          18..96
FT                   /note="MIT"
FT                   /evidence="ECO:0000259|SMART:SM00745"
FT   REGION          91..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  67837 MW;  3ECEBA0FC5213631 CRC64;
     MIIYFKLTLR FDFDSMILPP FKQKAIDLAS KAAQEDKAGN YEEALQLYQH AVQYFLHVVK
     YEAQGDKAKQ SIRAKCTEYL DRAEKLKEYL KKKEKKPQKP VKEGQPSPAD EKGNDSDGEG
     ESDDPEKKKL QNQLQGAIVI ERPNVKWSDV AGLEGAKEAL KEAVILPIKF PHLFTGVGVD
     NDGILVLGAT NIPWVLDSAI RRRFEKRIYI PLPEAHARAA MFKLHLGTTQ NSLTEADFRE
     LGKKTEGYSG ADISIIVRDA LMQPVRKVQS ATHFKKVHGP SRADPNSVVD DLLTPCSPGD
     PGAIEMTWMD VPGDKLLEPV VSMVTGGSSG IGKCIAIECY KQGAFITLVA RNEAQEKLGP
     VDMLVNCAGM AVSGKFEDLE VSSFERLMSV NYLGSVYPSR AVITTMKERR VGRIVFVSSQ
     AGQLGLFGFT AYSSSKFAIR GLAEALQMEV KPYNVYVTVA YPPDTDTPGF AEENKTKGLS
     SVQQLGSWEY RENGDAESQC PQGTWSRRCV NTVGQPLETR LISETTSVCK PEQVAKQIVK
     DAIQGNFNSS IGSDGYMLSS LTCGMAPVTS ITEGLQQVVT MGLFRTIALF YLGSFDSIIR
     RCMMQRARSE VADKTA
//
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