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Protein

Steroid C26-monooxygenase

Gene

cyp125

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25S)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.1 Publication

Catalytic activityi

Cholest-4-en-3-one + 3 NADH + 3 O2 = (25S)-3-oxocholest-4-en-26-oate + 3 NAD+ + 4 H2O.By similarity1 Publication

Cofactori

heme2 Publications

Kineticsi

  1. KM=14 µM for cholest-4-en-3-one1 Publication

    Pathwayi: cholesterol degradation

    This protein is involved in the pathway cholesterol degradation, which is part of Steroid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway cholesterol degradation and in Steroid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi360Iron (heme axial ligand)Combined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionMonooxygenase, Oxidoreductase
    Biological processCholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism
    LigandHeme, Iron, Metal-binding, NAD

    Enzyme and pathway databases

    UniPathwayiUPA01058.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Steroid C26-monooxygenase1 Publication (EC:1.14.13.141By similarity1 Publication)
    Alternative name(s):
    Cholest-4-en-3-one C26-monooxygenase1 Publication
    Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]By similarity1 Publication
    Cholesterol C26-monooxygenase1 Publication
    Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming]By similarity1 Publication
    Cytochrome P450 1251 Publication
    Steroid C27-monooxygenaseBy similarity
    Gene namesi
    Name:cyp1251 Publication
    Synonyms:cyp125A31 Publication
    Ordered Locus Names:MSMEG_5995Imported
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
    Proteomesi
    • UP000006158 Componenti: Chromosome
    • UP000000757 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show lower accumulation of 26-hydroxycholest-4-en-3-one and cholest-4-en-3-one-26-oate when compared with the wild-type and display a strong induction of cyp142A2. The levels of 26-hydroxycholest-4-en-3-one and cholest-4-on-3-one-26-oate are drastically reduced in cells lacking both cyp125A3 and cyp142A2.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004387231 – 427Steroid C26-monooxygenaseAdd BLAST427

    Expressioni

    Inductioni

    By cholesterol.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi246196.MSMEG_5995.

    Structurei

    Secondary structure

    1427
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 6Combined sources3
    Helixi15 – 20Combined sources6
    Helixi24 – 33Combined sources10
    Beta strandi35 – 40Combined sources6
    Turni46 – 48Combined sources3
    Beta strandi51 – 56Combined sources6
    Helixi59 – 67Combined sources9
    Turni69 – 71Combined sources3
    Beta strandi72 – 74Combined sources3
    Turni75 – 77Combined sources3
    Helixi89 – 93Combined sources5
    Helixi95 – 97Combined sources3
    Helixi99 – 101Combined sources3
    Helixi106 – 114Combined sources9
    Helixi115 – 118Combined sources4
    Helixi120 – 124Combined sources5
    Helixi127 – 142Combined sources16
    Beta strandi145 – 148Combined sources4
    Helixi149 – 152Combined sources4
    Turni153 – 155Combined sources3
    Helixi156 – 166Combined sources11
    Helixi170 – 172Combined sources3
    Helixi173 – 183Combined sources11
    Helixi189 – 191Combined sources3
    Helixi196 – 216Combined sources21
    Helixi222 – 227Combined sources6
    Helixi238 – 251Combined sources14
    Helixi254 – 269Combined sources16
    Helixi271 – 280Combined sources10
    Helixi285 – 293Combined sources9
    Beta strandi298 – 305Combined sources8
    Beta strandi307 – 309Combined sources3
    Beta strandi312 – 314Combined sources3
    Beta strandi319 – 323Combined sources5
    Helixi324 – 327Combined sources4
    Turni331 – 333Combined sources3
    Beta strandi334 – 336Combined sources3
    Beta strandi354 – 356Combined sources3
    Helixi363 – 380Combined sources18
    Beta strandi385 – 388Combined sources4
    Beta strandi396 – 398Combined sources3
    Beta strandi401 – 403Combined sources3
    Beta strandi405 – 412Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4APYX-ray2.00A1-427[»]
    5DQNX-ray2.26A1-426[»]
    ProteinModelPortaliA0R4Y3.
    SMRiA0R4Y3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    HOGENOMiHOG000243680.
    KOiK15981.
    OMAiDYTGKCP.
    OrthoDBiPOG091H0API.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiView protein in InterPro
    IPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    PfamiView protein in Pfam
    PF00067. p450. 1 hit.
    PRINTSiPR00359. BP450.
    SUPFAMiSSF48264. SSF48264. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A0R4Y3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPTPNIPSDF DFLDATLNLE RLPVEELAEL RKSEPIHWVD VPGGTGGFGD
    60 70 80 90 100
    KGYWLVTKHA DVKEVSRRSD VFGSSPDGAI PVWPQDMTRE AVDLQRAVLL
    110 120 130 140 150
    NMDAPQHTRL RKIISRGFTP RAIGRLEDEL RSRAQKIAQT AAAQGAGDFV
    160 170 180 190 200
    EQVSCELPLQ AIAELLGVPQ DDRDKLFRWS NEMTAGEDPE YADVDPAMSS
    210 220 230 240 250
    FELISYAMKM AEERAVNPTE DIVTKLIEAD IDGEKLSDDE FGFFVVMLAV
    260 270 280 290 300
    AGNETTRNSI THGMIAFAQN PDQWELYKKE RPETAADEIV RWATPVSAFQ
    310 320 330 340 350
    RTALEDVELG GVQIKKGQRV VMSYRSANFD EEVFEDPHTF NILRSPNPHV
    360 370 380 390 400
    GFGGTGAHYC IGANLARMTI NLIFNAIADN MPDLKPIGAP ERLKSGWLNG
    410 420
    IKHWQVDYTG AGKASVSGAP GTCPVAH
    Length:427
    Mass (Da):47,106
    Last modified:January 9, 2007 - v1
    Checksum:iD1C6EE17D397B8FD
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti1M → MHFEERTPM in AFP42267 (PubMed:17295914).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK74881.1.
    CP001663 Genomic DNA. Translation: AFP42267.1.
    RefSeqiWP_011730960.1. NZ_CP009494.1.
    YP_890221.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK74881; ABK74881; MSMEG_5995.
    AFP42267; AFP42267; MSMEI_5834.
    GeneIDi4531666.
    KEGGimsb:LJ00_29640.
    msg:MSMEI_5834.
    msm:MSMEG_5995.
    PATRICi18084223. VBIMycSme59918_5831.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000480 Genomic DNA. Translation: ABK74881.1.
    CP001663 Genomic DNA. Translation: AFP42267.1.
    RefSeqiWP_011730960.1. NZ_CP009494.1.
    YP_890221.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4APYX-ray2.00A1-427[»]
    5DQNX-ray2.26A1-426[»]
    ProteinModelPortaliA0R4Y3.
    SMRiA0R4Y3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi246196.MSMEG_5995.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABK74881; ABK74881; MSMEG_5995.
    AFP42267; AFP42267; MSMEI_5834.
    GeneIDi4531666.
    KEGGimsb:LJ00_29640.
    msg:MSMEI_5834.
    msm:MSMEG_5995.
    PATRICi18084223. VBIMycSme59918_5831.

    Phylogenomic databases

    HOGENOMiHOG000243680.
    KOiK15981.
    OMAiDYTGKCP.
    OrthoDBiPOG091H0API.

    Enzyme and pathway databases

    UniPathwayiUPA01058.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiView protein in InterPro
    IPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    PfamiView protein in Pfam
    PF00067. p450. 1 hit.
    PRINTSiPR00359. BP450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCP125_MYCS2
    AccessioniPrimary (citable) accession number: A0R4Y3
    Secondary accession number(s): I7G9K1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 18, 2017
    Last sequence update: January 9, 2007
    Last modified: April 12, 2017
    This is version 79 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.