ID   A0A182MUQ5_9DIPT        Unreviewed;       901 AA.
AC   A0A182MUQ5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=Sarcosine dehydrogenase, mitochondrial {ECO:0008006|Google:ProtNLM};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA026693-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA026693-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA026693-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; AXCM01005411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182MUQ5; -.
DR   STRING; 139723.A0A182MUQ5; -.
DR   EnsemblMetazoa; ACUA026693-RA; ACUA026693-PA; ACUA026693.
DR   VEuPathDB; VectorBase:ACUA026693; -.
DR   OrthoDB; 1815533at2759; -.
DR   Proteomes; UP000075883; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR032503; FAO_M.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF200; SARCOSINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16350; FAO_M; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          48..406
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          411..463
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          468..782
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          805..890
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   901 AA;  100095 MW;  B1BF8D982FB906AA CRC64;
     MLRLRTQAVA KFKSHLLGGD RQSAISAAAI ATANRTYATE SPVPESADVV IIGGGSAGCN
     TLYQLAKRGV RAVLLEKSKL TAGTTWHTAG LVWRLRPNDV EIRLLAATRD LLMSLEEETG
     QNSGWINNGG LFISHSPERL DEYSRLATLG KCFGIESHII GPEEAQKIFP PLDPSSFTGA
     LYSPGDGVVD PAMMCTALTK GATANGGRVI EECTVTQIIT GENLLGMKDV RGVLTNKGMI
     RTNTVVNATG VWGRDLIEPL GVFLPLIPMK HAYVVSETMD TIHQMLPNVR DHDFSLYFRI
     QGKSICMGGY ENNPILLNRV PGDFHFGLYD LDYSVFDTHI QGAVKLCPAF GSAGIKSTIC
     GPESFTPDHK PLMGPDPTVS GLFHSVGYNS AGMMLGGGCA EQLAKWIINE RPDRHMFAYD
     VRRFTPKQKK ALNWATERSH EAYAKNYSIV FPHDEPLAGR NFTVDPFHKQ MIQYGAVMEE
     RHGWERPGYF LPDETVVVQP YDWYGYYDHP KNANTHYEEA LKGDYTFGFS EHHDLIGEEA
     LTCRHDAALF NLSYFCKLFL TGSQAKEAAE WIFTANLDKP INKTVYTCAL NKNGGVEGDV
     TVSIVESGLG GLHDPIFKGR GYYIVAGGAS AYHTKCHILS AIQEKAFRAV VSDHTEELGV
     LSLQGPKSRD ILQKITDFDL SNEQLLPLNS TAILTIKINP HYSCNVRVLR VSFVGELGYE
     LHIPEESCND VYNALMKAGY KESLRNAGYR ALYSLSSEKG YHLWGFDLRS DDTPIEANLG
     FVCRKNGEYQ GKEIIDRQRE NGVNRRLAFF TVRDQVPIWG LEAVYRDGEI VGHLRRGEYG
     YTLQKPIGQA YVQRSDGSPI TNQFLQSGRY QIEVMGKLYD ADCHLRSPFD PKGERLLGIY
     K
//